Sandbox Reserved 489: Difference between revisions

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[[Image:2RenCartoon.png|thumb|400px|alt=text|Renin]]

Renin, also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1. Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site in a reduction-oxidation reaction with water to specifically cleave peptide substrates. Mature renin circulates in the blood and contains 340 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave ~~the angiotensin I precursor,~~ angiotensinogen, to produce angiotensin I.

Renin, also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1. Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site in a reduction-oxidation reaction with water to specifically cleave peptide substrates. Mature renin circulates in the blood stream and contains 340 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave angiotensinogen to produce angiotensin I.

Renin is secreted by the kidneys. The kidneys act both directly and indirectly to regulate arterial blood pressure and provide the major long term mechanism of blood pressure and control. The direct mechanism changes blood volume independently of hormones. When blood pressure and blood volume increase the kidneys can not filter all of the liquids and thus liquids are lost in the urine to decrease blood pressure and blood volume.

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The indirect mechanism, or the [http://en.wikipedia.org/wiki/Renin-angiotensin_system renin-angiotensin system] (RAS), controls blood volume and blood pressure through renin and two forms of [http://en.wikipedia.org/wiki/Angiotensin angiotensin]. Renin is involved in the rate limiting first step of a cascade that eventually produces angiotensin II. The specialized granular cells of the [http://en.wikipedia.org/wiki/Juxtaglomerular_apparatus juxtaglomerular apparatus] secrete renin when stimulated by the [http://en.wikipedia.org/wiki/Macula_densa macula densa] when blood pressure or blood volume decreases. Renin circulating in the blood stream cleaves a small 10 residue portion of plasma protein angiotensinogen that is secreted by the liver. Cleavage of angiotensinogen produces the inactive precursor angiotensin I that is converted to angiotensin II by [http://en.wikipedia.org/wiki/Angiotensin-converting_enzyme angiotensin-converting enzyme] primarily in the lungs. Angiotensin II increases blood pressure in three ways.

:*Angiotensin II constricts blood vessels by influencing smooth muscle tissue. The heart pumps faster to overcome the constricted arteries and blood pressure rises.

:*Angiotensin II stimulates the [http://en.wikipedia.org/wiki/Adrenal_cortex adrenal cortex] to secrete [http://en.wikipedia.org/wiki/Aldosterone aldosterone] that causes renal adsorption of sodium. ~~when~~ sodium moves into the blood stream water follows to increase the blood volume.

:*Angiotensin II stimulates the [http://en.wikipedia.org/wiki/Adrenal_cortex adrenal cortex] to secrete [http://en.wikipedia.org/wiki/Aldosterone aldosterone] that causes renal adsorption of sodium. When sodium moves into the blood stream water follows to increase the blood volume.

:*Angiotensin II causes the [http://en.wikipedia.org/wiki/Posterior_pituitary posterior pituitary gland] to release [http://en.wikipedia.org/wiki/Vasopressin vasopressin], also known as antidiuretic hormone, to induce water reabsorption.

Additionally, angiotensin II triggers the sensation of thirst.

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The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet</scene> that forms the two similar lobes of renin. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic (blue) and hydrophobic (red) residues</scene> are located primarily on the outside and inside portions of renin respectively. The most important structure is the <scene name='Sandbox_Reserved_489/Hydrophobicactivesite/1'>hydrophobic pocket</scene> located in the active site that allows substrate binding. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>. Renin has <scene name='Sandbox_Reserved_489/Catalyticmotifs/1'>two catalytic motifs</scene> after each of the two aspartate residues. Renin also uses a <scene name='Sandbox_Reserved_489/Activesiteflap/1'>active site flap</scene>, a beta hairpin structure, that open and closes to uncover or cover the active site.

The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'> 2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet</scene> that forms the two similar lobes of renin. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic (blue) and hydrophobic (red) residues</scene> are located primarily on the outside and inside portions of renin respectively. The most important structure is the <scene name='Sandbox_Reserved_489/Hydrophobicactivesite/1'>hydrophobic pocket</scene> located in the active site that allows substrate binding. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>. Renin has <scene name='Sandbox_Reserved_489/Catalyticmotifs/1'>two catalytic motifs</scene> after each of the two aspartate residues. Renin also uses a <scene name='Sandbox_Reserved_489/Activesiteflap/1'>active site flap</scene>, a beta hairpin structure, that open and closes to uncover or cover the active site.

Post translational modifications of renin include; precursor cleavage of propetide to produce active mature renin, disulfide bond formation, and glycosylation of certain residues. Disulfide bonds are form to connect serine residues <scene name='Sandbox_Reserved_489/Disulfidebond1/1'>51 to 58</scene>, <scene name='Sandbox_Reserved_489/Disulfidebond2/1'>217 to 221</scene>, and <scene name='Sandbox_Reserved_489/Disulfidebond3/1'>259 to 296</scene>. <scene name='Sandbox_Reserved_489/Glycosylated/2'>Two asparagine residues</scene> at positions 14 and 75 can be glycosylated. The asparagine residue at postion 75 is glycosylated (2-(acetylamino)-2-deoxy-A-D-glucopyranose) in mature renin whereas the residue at postion 14 is not glycosylated.<ref>Margrane M. and the UnitProt consortium, '''Uniprot Knowledgebase: a hub of integrated protein data''', Database, 2012: bar009 (2011). Public Accession Number P00797 </ref>

Sandbox Reserved 489: Difference between revisions

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@@ Line 7: / Line 7: @@
 [[Image:2RenCartoon.png|thumb|400px|alt=text|Renin]]
-Renin, also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1.  Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site in a reduction-oxidation reaction with water to specifically cleave peptide substrates.  Mature renin circulates in the blood and contains 340 amino acid residues and has a mass of approximately 37 kDa.  The function of renin is to cleave the angiotensin I precursor, angiotensinogen, to produce angiotensin I.
+Renin, also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1.  Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site in a reduction-oxidation reaction with water to specifically cleave peptide substrates.  Mature renin circulates in the blood stream and contains 340 amino acid residues and has a mass of approximately 37 kDa.  The function of renin is to cleave angiotensinogen to produce angiotensin I.
 Renin is secreted by the kidneys.  The kidneys act both directly and indirectly to regulate arterial blood pressure and provide the major long term mechanism of blood pressure and control.  The direct mechanism changes blood volume independently of hormones.  When blood pressure and blood volume increase the kidneys can not filter all of the liquids and thus liquids are lost in the urine to decrease blood pressure and blood volume.
@@ Line 13: / Line 13: @@
 The indirect mechanism, or the [http://en.wikipedia.org/wiki/Renin-angiotensin_system renin-angiotensin system]  (RAS), controls blood volume and blood pressure through renin and two forms of [http://en.wikipedia.org/wiki/Angiotensin angiotensin].  Renin is involved in the rate limiting first step of a cascade that eventually produces angiotensin II.  The specialized granular cells of the [http://en.wikipedia.org/wiki/Juxtaglomerular_apparatus juxtaglomerular apparatus] secrete renin when stimulated by the [http://en.wikipedia.org/wiki/Macula_densa macula densa] when blood pressure or blood volume decreases.  Renin circulating in the blood stream cleaves a small 10 residue portion of plasma protein angiotensinogen that is secreted by the liver.  Cleavage of angiotensinogen produces the inactive precursor angiotensin I that is converted to angiotensin II by [http://en.wikipedia.org/wiki/Angiotensin-converting_enzyme angiotensin-converting enzyme] primarily in the lungs.  Angiotensin II increases blood pressure in three ways.
 :*Angiotensin II constricts blood vessels by influencing smooth muscle tissue. The heart pumps faster to overcome the constricted arteries and blood pressure rises.
-:*Angiotensin II  stimulates the [http://en.wikipedia.org/wiki/Adrenal_cortex adrenal cortex] to secrete [http://en.wikipedia.org/wiki/Aldosterone aldosterone] that causes renal adsorption of sodium.  when sodium moves into the blood stream water follows to increase the blood volume.
+:*Angiotensin II  stimulates the [http://en.wikipedia.org/wiki/Adrenal_cortex adrenal cortex] to secrete [http://en.wikipedia.org/wiki/Aldosterone aldosterone] that causes renal adsorption of sodium.  When sodium moves into the blood stream water follows to increase the blood volume.
 :*Angiotensin II causes the [http://en.wikipedia.org/wiki/Posterior_pituitary posterior pituitary gland] to release [http://en.wikipedia.org/wiki/Vasopressin vasopressin], also known as antidiuretic hormone, to induce water reabsorption.
 Additionally, angiotensin II triggers the sensation of thirst.
@@ Line 26: / Line 26: @@
 <Structure load='2ren' size='400' frame='true' align='left' caption='Mature Renin' scene='Insert optional scene name here' />
-The precursor of renin is a 406 amino acid residue protein.  <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>.  The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>.  The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet</scene> that forms the two similar lobes of renin.  <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic (blue) and hydrophobic (red) residues</scene> are located primarily on the outside and inside portions of renin respectively.  The most important structure is the <scene name='Sandbox_Reserved_489/Hydrophobicactivesite/1'>hydrophobic pocket</scene> located in the active site that allows substrate binding. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>.  Renin has <scene name='Sandbox_Reserved_489/Catalyticmotifs/1'>two catalytic motifs</scene> after each of the two aspartate residues.  Renin also uses a <scene name='Sandbox_Reserved_489/Activesiteflap/1'>active site flap</scene>, a beta hairpin structure, that open and closes to uncover or cover the active site.
+The precursor of renin is a 406 amino acid residue protein.  <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>.  The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'> 2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>.  The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet</scene> that forms the two similar lobes of renin.  <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic (blue) and hydrophobic (red) residues</scene> are located primarily on the outside and inside portions of renin respectively.  The most important structure is the <scene name='Sandbox_Reserved_489/Hydrophobicactivesite/1'>hydrophobic pocket</scene> located in the active site that allows substrate binding. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>.  Renin has <scene name='Sandbox_Reserved_489/Catalyticmotifs/1'>two catalytic motifs</scene> after each of the two aspartate residues.  Renin also uses a <scene name='Sandbox_Reserved_489/Activesiteflap/1'>active site flap</scene>, a beta hairpin structure, that open and closes to uncover or cover the active site.
 Post translational modifications of renin include; precursor cleavage of propetide to produce active mature renin, disulfide bond formation, and glycosylation of certain residues.  Disulfide bonds are form to connect serine residues <scene name='Sandbox_Reserved_489/Disulfidebond1/1'>51 to 58</scene>, <scene name='Sandbox_Reserved_489/Disulfidebond2/1'>217 to 221</scene>, and <scene name='Sandbox_Reserved_489/Disulfidebond3/1'>259 to 296</scene>.  <scene name='Sandbox_Reserved_489/Glycosylated/2'>Two asparagine residues</scene> at positions 14 and 75 can be glycosylated. The asparagine residue at postion 75 is glycosylated (2-(acetylamino)-2-deoxy-A-D-glucopyranose) in mature renin whereas the residue at postion 14 is not glycosylated.<ref>Margrane M. and the UnitProt consortium, '''Uniprot Knowledgebase: a hub of integrated protein data''', Database, 2012: bar009 (2011). Public Accession Number P00797 </ref>