https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Drew+BarberProteopedia - User contributions [en]2026-09-16T10:08:43ZUser contributionsMediaWiki 1.43.8https://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922416Sandbox Reserved 1862014-04-30T14:22:01Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1) [[Image:Reaction_of_GPx-1.jpg|100px|right|thumb|]]. In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. The overall fold of GPx-1 is similar to that of thioredoxin. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS) (7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (11). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (11). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (11). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Martin JL (1995). Thioredoxin-a fold for all reasons. Structure 3(3), 245-250.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.Pan JL, Bardwell JCA (2006). The origami of thioredoxin-like folds. Protein Science 15(10), 2217-2227.</div>Drew Barberhttps://proteopedia.org/index.php?title=File:Reaction_of_GPx-1.jpg&diff=1922415File:Reaction of GPx-1.jpg2014-04-30T14:21:02Z<p>Drew Barber: Figure 1. Reaction catalyzed by GPx-1. 1. The peroxidatic Selenocysteine residue reacts with hydrogen peroxide. This yields one molecule of water and the selenenic acid form of the peroxidatic residue (Se-OH). 2. One molecule of glutathione (GSH) react</p>
<hr />
<div>Figure 1. Reaction catalyzed by GPx-1. 1. The peroxidatic Selenocysteine residue reacts with hydrogen peroxide. This yields one molecule of water and the selenenic acid form of the peroxidatic residue (Se-OH). 2. One molecule of glutathione (GSH) reacts with Se-OH which yields the second water molecule and the and an enzyme glutathione complex (Se-SG). 3. A second molecule of GSH reacts with the Se-SG complex yielding a regenerated enzyme and oxidized glutathione (GS-SG).</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922411Sandbox Reserved 1862014-04-30T13:49:35Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. The overall fold of GPx-1 is similar to that of thioredoxin. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS) (7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (11). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (11). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (11). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Martin JL (1995). Thioredoxin-a fold for all reasons. Structure 3(3), 245-250.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.Pan JL, Bardwell JCA (2006). The origami of thioredoxin-like folds. Protein Science 15(10), 2217-2227.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922410Sandbox Reserved 1862014-04-30T13:47:32Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. The overall fold of GPx-1 is similar to that of thioredoxin. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS) (7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (11). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (11). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (11). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Martin JL (1995). Thioredoxin-a fold for all reasons. Structure 3(3), 245-250.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922409Sandbox Reserved 1862014-04-30T13:46:50Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. The overall fold of GPx-1 is similar to that of thioredoxin. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS) (7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Martin JL (1995). Thioredoxin-a fold for all reasons. Structure 3(3), 245-250.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922408Sandbox Reserved 1862014-04-30T13:42:53Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. The overall fold of GPx-1 is similar to that of thioredoxin. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS) (7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922407Sandbox Reserved 1862014-04-30T13:40:44Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS) (7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922406Sandbox Reserved 1862014-04-30T13:40:19Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS) (7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922405Sandbox Reserved 1862014-04-30T13:38:49Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.<br />
<br />
9.Khanna KK, Jackson SP (2001). DNA double-stranded breaks: signaling, repair and the caner connection. Nature Genetics 27, 247-54.<br />
<br />
10.Driessens N, Verteyhe S, Ghaddhab C, Burniat A, Deken XD, Sande J, Dumont JE, Miot F, Corvilain B (2009). Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr Relat Cancer 16, 845-56.<br />
<br />
11.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922404Sandbox Reserved 1862014-04-30T13:32:59Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H2O + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922402Sandbox Reserved 1862014-04-30T13:31:46Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(7,8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.<br />
<br />
7. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal, BB (2010). Oxidative stress, inflammation and cancer: how are they linked? Free Radical Biology and Medicine 49, 1603-1616.<br />
<br />
8. Barnham KJ, Masters CL, Bush AI (2004). Neurodegenerative diseases and oxidative stress. Nature Reviews Drug Discovery 3, 205-214.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922401Sandbox Reserved 1862014-04-30T13:29:38Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (4). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(7). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (8,9). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (10). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (11). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (11). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (11). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4.Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5.Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6.Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922396Sandbox Reserved 1862014-04-30T13:20:06Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (7). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
<br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
<br />
4. Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
<br />
5. Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
<br />
6. Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922395Sandbox Reserved 1862014-04-30T13:19:41Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (7). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
1.Lubos E, Loscalzo J, Handy DE (2011). Glutathione Peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15 (7), 1958-1982.<br />
2.Prabhakar R, Vreven T, Morokuma K, Musaev DG (2005). Elucidation of the mechanism of selenoprotein glutathione peroxidase (Gpx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871. <br />
3.Marinho HS, Antunes F, Pinto RE (1997). Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med 22, 871-883.<br />
4. Roman M, Jitaru P, Barbante C (2014). Selenium biochemistry and its role for human health. Metallomics 6, 25-54.<br />
5. Berndt C, Lillig CH, Holmgren A (2008). Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783, 641-650.<br />
6. Atkinson HJ, Babbitt PC (2009). An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLOS computational biology, epub.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922394Sandbox Reserved 1862014-04-30T13:18:36Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (7). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922393Sandbox Reserved 1862014-04-30T13:17:23Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (7). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
Proteins that have a thioredoxin like fold are involved in catalyzing reduction, oxidation, or disulfide bond exchanges (11). Thioredoxin is the protein after which the fold is named and is an important redox protein. Glutaredoxins are another class of proteins that have a thioredoxin like fold and are distantly related to thioredoxin. This family of proteins are also involved in maintaining the redox state of the cytosol (12). A third class of proteins with this fold are the disulfide oxidoreductases which are involved in catalyzing the formation of disulfide bonds and play an important role in protein folding (12). Glutathione peroxidases also have a thioredoxin like fold and are involved in the reduction of various oxidants which helps to modulate the intracellular redox state. Peroxyredoxins are also involved in the regulation of the intracellular redox state as they reduce various peroxides. A final class of proteins that contain a thioredoxin like fold are the glutathione-s-transferases which catalyze the transfer of glutathione to various substrates and which is an important step in the metabolism of various molecules (12). <br />
<br />
<br />
<br />
<br />
<br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1922389Sandbox Reserved 1862014-04-30T12:57:56Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These diseases include cancers, neurodegenerative diseases, heart disease, and diabetes (7). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
<br />
<br />
<br />
<br />
<br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1920214Sandbox Reserved 1862014-04-30T07:43:19Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
Because of its role as an anti-oxidant, deficiencies in GPx-1 have been linked to the pathogenesis of multiple diseases. These disease include cancers, neurodegenerative diseases, heart disease, and diabetes (7). The Pathogenisis of these diseases have been linked to the presences of excessive reactive oxygen species (ROS)(8). One major oxidant is hydrogen peroxide which has been shown to oxidatively modify proteins and DNA bases as well as induce single and double stranded DNA breaks (9,10). Deficiencies in GPx-1 could result in excessive hydrogen peroxide and thus cellular damage giving rise to these disorders.<br />
<br />
== Other Proteins with a thioredoxin like fold ==<br />
<br />
<br />
<br />
<br />
<br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1920089Sandbox Reserved 1862014-04-30T07:35:35Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== GPx-1 and Disease ==<br />
<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1920087Sandbox Reserved 1862014-04-30T07:34:47Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4)[[Image:Thioredoxin_fold.jpg|100px|left|thumb|]] (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=File:Thioredoxin_fold.jpg&diff=1920086File:Thioredoxin fold.jpg2014-04-30T07:31:59Z<p>Drew Barber: Figure 4. Thioredoxin Fold. Red arrows represent B-sheets while blue rectangles represent alpha-helices. A. Thioredoxin fold. B. Fold of glutathione peroxidase.</p>
<hr />
<div>Figure 4. Thioredoxin Fold. Red arrows represent B-sheets while blue rectangles represent alpha-helices. A. Thioredoxin fold. B. Fold of glutathione peroxidase.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1920077Sandbox Reserved 1862014-04-30T06:49:58Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|100px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|100px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4) (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|100px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1920076Sandbox Reserved 1862014-04-30T06:47:26Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold of GPx-1 ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|300px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (Figure 4) (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (Figure 5)[[Image:Thioredoxin_like_fold.jpg|300px|right|thumb|]] (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=File:Thioredoxin_like_fold.jpg&diff=1919988File:Thioredoxin like fold.jpg2014-04-30T06:43:57Z<p>Drew Barber: Figure 5. Thioredoxin lik fold of GPx-1. Purple sequences are n-term to thioredoxin like fold. Blue sequences represent classic thioredoxin architecture. Red sequences are secondary structures insertions in the thioredoxin fold.</p>
<hr />
<div>Figure 5. Thioredoxin lik fold of GPx-1. Purple sequences are n-term to thioredoxin like fold. Blue sequences represent classic thioredoxin architecture. Red sequences are secondary structures insertions in the thioredoxin fold.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1919437Sandbox Reserved 1862014-04-30T05:34:12Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with five of the helices being of the 310 form (Figure 2)[[Image:Helix310.jpg|300px|left|thumb|]]. Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. GPx-1 exhibits a thioredoxin like fold. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides(6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=File:Helix310.jpg&diff=1919403File:Helix310.jpg2014-04-30T05:32:44Z<p>Drew Barber: Figure 2. A 3 10 helix from GPx-1 (PDB id: 2F8A)</p>
<hr />
<div>Figure 2. A 3 10 helix from GPx-1 (PDB id: 2F8A)</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1919089Sandbox Reserved 1862014-04-30T05:18:26Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
The secondary structure of GPx-1 consists of nine β-strands and nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918983Sandbox Reserved 1862014-04-30T05:14:05Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918971Sandbox Reserved 1862014-04-30T05:13:42Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>TextToBeDisplayed</scene>' size='350' frame='true' align='right' <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918955Sandbox Reserved 1862014-04-30T05:12:56Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/2'>TextToBeDisplayed</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918930Sandbox Reserved 1862014-04-30T05:10:23Z<p>Drew Barber: </p>
<hr />
<div>lycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> <br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918929Sandbox Reserved 1862014-04-30T05:09:52Z<p>Drew Barber: </p>
<hr />
<div>==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918928Sandbox Reserved 1862014-04-30T05:08:31Z<p>Drew Barber: </p>
<hr />
<div><br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918926Sandbox Reserved 1862014-04-30T05:07:15Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Glutathione Peroxidase 1==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918925Sandbox Reserved 1862014-04-30T05:06:54Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Glutathione Peroxidase 1)==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918923Sandbox Reserved 1862014-04-30T05:05:03Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918922Sandbox Reserved 1862014-04-30T05:04:34Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|left|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918921Sandbox Reserved 1862014-04-30T05:02:27Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).[[Image:Beta_sheets3.jpg|300px|left|thumb|]]<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=File:Beta_sheets3.jpg&diff=1918920File:Beta sheets3.jpg2014-04-30T05:01:59Z<p>Drew Barber: Figure 3. Parallel and anti-parallel beta-sheets. A. Parallel beta-sheets represented as cartoon or sticks. Hydrogen bonding is indicated by dashed lines. B. Anti-parallel beta-sheets represented as cartoon or sticks. Hydrogen bonding is indicated by</p>
<hr />
<div>Figure 3. Parallel and anti-parallel beta-sheets. A. Parallel beta-sheets represented as cartoon or sticks. Hydrogen bonding is indicated by dashed lines. B. Anti-parallel beta-sheets represented as cartoon or sticks. Hydrogen bonding is indicated by dashed lines.</div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918917Sandbox Reserved 1862014-04-30T04:53:23Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).[[Image:Beta sheets 2.jpg|900px|left|thumb|]]<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918916Sandbox Reserved 1862014-04-30T04:52:09Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).[[Image:Beta sheets 2.jpg|left|]]<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918915Sandbox Reserved 1862014-04-30T04:51:19Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).[[Image:Beta sheets 2.jpg|left|thumb|]]<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918914Sandbox Reserved 1862014-04-30T04:46:33Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).[[Image:Beta sheets 2.jpg]]<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918913Sandbox Reserved 1862014-04-30T04:45:49Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).[[Image:Beta sheets 2.jpg] frame='true' align='right']<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918912Sandbox Reserved 1862014-04-30T04:44:11Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).[[Image:Beta sheets 2.jpg]]<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918910Sandbox Reserved 1862014-04-30T04:41:02Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet[[Image:Beta sheets 2.jpg]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918908Sandbox Reserved 1862014-04-30T04:38:37Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet[[Image:Beta sheets2]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918907Sandbox Reserved 1862014-04-30T04:38:13Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet[[Image:Beta sheets2.jpg]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918904Sandbox Reserved 1862014-04-30T04:31:26Z<p>Drew Barber: </p>
<hr />
<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
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<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
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== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet[[Image:Beta sheets.jpg]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
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== Relevance ==<br />
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== Structural highlights ==<br />
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
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</StructureSection><br />
== References ==<br />
<references/></div>Drew Barberhttps://proteopedia.org/index.php?title=Sandbox_Reserved_186&diff=1918903Sandbox Reserved 1862014-04-30T04:29:36Z<p>Drew Barber: </p>
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<div><Structure load='<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<br />
<br />
<scene name='58/583431/Gpx-1/1'>Glycine Mutant of Glutatione Peroxidase 1</scene><br />
== Overview ==<br />
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).<br />
<br />
== Secondary Structure and the Thioredoxin Like Fold ==<br />
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet[<Structure load=Beta sheets.jpg' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />]. Overall GPx-1 exhibits a thioredoxin like fold (Figure 2). The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Drew Barber