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https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Mary+Lively Proteopedia - User contributions [en] 2026-10-04T22:57:28Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3679786 Sandbox Reserved 1732 2022-12-09T02:51:22Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> =='''Insulin Receptor'''==<br /> <Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' /><br /> <scene name='91/919041/Insulin_Receptor/1'></scene><br /> <br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions <ref>Pubmed</ref>.The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation <ref>Pubmed</ref>.<br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor <ref>Pubmed</ref>. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium <ref>Pubmed</ref>. <br /> <br /> == Disease ==<br /> Diseases that involve insulin receptors are normally due to wrong signaling. Insulin regulates blood glucose levels, and with no regulation, it will lead to diseases such as obesity, type I and type II diabetes. Diabetes mainly happens due to elevated levels of blood glucose levels which can result in serious complications over time if not treated correctly. Insulin receptors will interact with cell surface insulin as a mediator of signaling. Around 10.5% of the US population have diabetes. Most of them have type II diabetes. This type of diabetes is considerably more dangerous as it has to do with lifestyle and not the disease coming from a genetic condition that shows up early in life. People with type II diabetes are more susceptive to being obese due to their lifestyle <ref>Pubmed</ref>. <br /> <br /> == Relevance ==<br /> Insulin secretion and binding to the insulin receptor initiates a robust physiological response in a healthy individual. The correct insulin signaling is important as it regulates many things that include glucose, lipid, and energy homeostasis. Diseases that happen relating to insulin are due to wrong signaling. These include type I diabetes and type II diabetes. Type I diabetes is normally associated with a genetic condition that shows up early in life. Type II diabetes is normally due to a certain unhealthy lifestyle and will develop over time <ref>Pubmed</ref>. <br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the Juxtamembrane domain, and the intracellular tyrosine kinase domain <ref>Pubmed</ref>. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. Site L1' is dark green, CR' is orange, L2' is light blue, L2 is yellow, CR is red, L1 is dark blue, β-subunits are brown and light pink, insulin bound to the receptor is hot pink.<ref>http://biorxiv.org/</ref> <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.The beta subunits consist of Fibronectin domain III-2 (FnIII-2) and Fibronectin domain III-3 (FnIII-3). In the image below, Sites 1 and 1' are green. Sites 2 and 2' are red <ref>Pubmed</ref>. <br /> <br /> [[Image:biochemIBSpt2.png]]<br /> <br /> There are two main conformations of full-length insulin receptors, U-shaped and T-shaped. The U-shaped conformation exists when there is an absence of insulin on the protein, whereas the T-shaped and II-shaped conformations exist in the presence of insulin. The U-shaped conformation is also known as the auto-inhibited state. In this state, the L1 domain contacts the L1’ and L2’ domains of the partnering protein. When insulin binds to the receptor protein, it causes a conformational change from the U-shape to the T-shape conformation <ref>Pubmed</ref>. <br /> <br /> == References ==<br /> <br /> 1 Goodsell, D. PDB101: Molecule of the month: Insulin receptor. https://pdb101.rcsb.org/motm/182 (accessed Nov 7, 2022).<br /> <br /> 2 PF;, L.J.P. (no date) The insulin receptor: Structure, function, and signaling, The American journal of physiology. U.S. National Library of Medicine. Available at: https://pubmed.ncbi.nlm.nih.gov/8141246/ (Accessed: October 21, 2022). <br /> <br /> 3 Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022).<br /> <br /> 4 PDB101: Global health: Diabetes mellitus: Drugs: Insulin: Insulin receptor https://pdb101.rcsb.org/global-health/diabetes-mellitus/drugs/insulin/insulin-receptor#:~:text=Insulin%20receptors%20are%20proteins%20found,metabolic%20and%20growth%2Drelated%20functions. (accessed Oct 21, 2022).<br /> <br /> 5 Boucher, Jérémie. Kleinridders, André. Kahn1, C. Ronald. Insulin Receptor Signaling in Normal and Insulin-Resistant States. https://cshperspectives.cshlp.org/content/6/1/a009191 (accessed Nov 14, 2022).<br /> <br /> 6 Scapin, G.; Dandey, V. P.; Zhang, Z.; Prosise, W.; Hruza, A.; Kelly, T.; Mayhood, T.; Strickland, C.; Potter, C. S.; Carragher, B. Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis. https://www.nature.com/articles/nature26153 (accessed Nov 7, 2022). <br /> <br /> 7 Kasago, Masuta. Hedo, Jose A. Yamada, Kenneth M. Kahn, C. Ronald. The Structure of Insulin Receptor and Its Subunits. https://www.jbc.org/article/S0021-9258(18)34032-8/pdf (accessed Oct 21, 2022).<br /> <br /> 8 Lee, J. and Pilch, P. F. The insulin receptor: structure, function, and signaling. https://journals.physiology.org/doi/abs/10.1152/ajpcell.1994.266.2.c319 (accessed Oct 21, 2022). <br /> <br /> 9 Lee, Yong Hee and Morris F. White. Insulin Receptor Substrate Proteins and Diabetes. https://link.springer.com/content/pdf/10.1007/BF02980074.pdf (accessed Nov 14, 2022)<br /> <br /> 10 Lawrence, M. C. Understanding insulin and its receptor from their three-dimensional structures https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513149/#bib1 (accessed Oct 21, 2022).<br /> <br /> <br /> 11 Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3672081 Sandbox Reserved 1732 2022-11-28T12:52:39Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> =='''Insulin Receptor'''==<br /> <Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' /><br /> <scene name='91/919041/Insulin_Receptor/1'></scene><br /> <br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> <br /> == Disease ==<br /> Diseases that involve insulin receptors are normally due to wrong signaling. Insulin regulates blood glucose levels, and with no regulation, it will lead to diseases such as obesity, type I and type II diabetes. Diabetes mainly happens due to elevated levels of blood glucose levels which can result in serious complications over time if not treated correctly. Insulin receptors will interact with cell surface insulin as a mediator of signaling. Around 10.5% of the US population have diabetes. Most of them have type II diabetes. This type of diabetes is considerably more dangerous as it has to do with lifestyle and not the disease coming from a genetic condition that shows up early in life. People with type II diabetes are more susceptive to being obese due to their lifestyle. <br /> <br /> == Relevance ==<br /> Insulin secretion and binding to the insulin receptor initiates a robust physiological response in a healthy individual. The correct insulin signaling is important as it regulates many things that include glucose, lipid, and energy homeostasis. Diseases that happen relating to insulin are due to wrong signaling. These include type I diabetes and type II diabetes. Type I diabetes is normally associated with a genetic condition that shows up early in life. Type II diabetes is normally due to a certain unhealthy lifestyle and will develop over time. <br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. Site L1' is dark green, CR' is orange, L2' is light blue, L2 is yellow, CR is red, L1 is dark blue, β-subunits are brown and light pink, insulin bound to the receptor is hot pink.<ref>http://biorxiv.org/</ref> <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.The beta subunits consist of Fibronectin domain III-2 (FnIII-2) and Fibronectin domain III-3 (FnIII-3). In the image below, Sites 1 and 1' are green. Sites 2 and 2' are red. <br /> <br /> [[Image:biochemIBSpt2.png]]<br /> <br /> There are two main conformations of full-length insulin receptors, U-shaped and T-shaped. The U-shaped conformation exists when there is an absence of insulin on the protein, whereas the T-shaped and II-shaped conformations exist in the presence of insulin. The U-shaped conformation is also known as the auto-inhibited state. In this state, the L1 domain contacts the L1’ and L2’ domains of the partnering protein. When insulin binds to the receptor protein, it causes a conformational change from the U-shape to the T-shape conformation. <br /> <br /> == References ==<br /> <br /> 1 Boucher, Jérémie. Kleinridders, André. Kahn1, C. Ronald. Insulin Receptor Signaling in Normal and Insulin-Resistant States. https://cshperspectives.cshlp.org/content/6/1/a009191 (accessed Nov 14, 2022).<br /> <br /> 2 Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 3 Goodsell, D. PDB101: Molecule of the month: Insulin receptor. https://pdb101.rcsb.org/motm/182 (accessed Nov 7, 2022). <br /> <br /> Home - PMC - NCBI https://www.ncbi.nlm.nih.gov/pmc/ (accessed Oct 21, 2022). <br /> <br /> 4 Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 5 Kasago, Masuta. Hedo, Jose A. Yamada, Kenneth M. Kahn, C. Ronald. The Structure of Insulin Receptor and Its Subunits. https://www.jbc.org/article/S0021-9258(18)34032-8/pdf (accessed Oct 21, 2022).<br /> <br /> 6 Lawrence, M. C. Understanding insulin and its receptor from their three-dimensional structures https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513149/#bib1 (accessed Oct 21, 2022). <br /> <br /> 7 Lee, J. and Pilch, P. F. The insulin receptor: structure, function, and signaling. https://journals.physiology.org/doi/abs/10.1152/ajpcell.1994.266.2.c319 (accessed Oct 21, 2022). <br /> <br /> 8 Lee, Yong Hee and Morris F. White. Insulin Receptor Substrate Proteins and Diabetes. https://link.springer.com/content/pdf/10.1007/BF02980074.pdf (accessed Nov 14, 2022)<br /> <br /> 9 PDB101: Global health: Diabetes mellitus: Drugs: Insulin: Insulin receptor https://pdb101.rcsb.org/global-health/diabetes-mellitus/drugs/insulin/insulin-receptor#:~:text=Insulin%20receptors%20are%20proteins%20found,metabolic%20and%20growth%2Drelated%20functions. (accessed Oct 21, 2022). <br /> <br /> 10 PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 11 PF;, L.J.P. (no date) The insulin receptor: Structure, function, and signaling, The American journal of physiology. U.S. National Library of Medicine. Available at: https://pubmed.ncbi.nlm.nih.gov/8141246/ (Accessed: October 21, 2022). <br /> <br /> 12 Scapin, G.; Dandey, V. P.; Zhang, Z.; Prosise, W.; Hruza, A.; Kelly, T.; Mayhood, T.; Strickland, C.; Potter, C. S.; Carragher, B. Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis. https://www.nature.com/articles/nature26153 (accessed Nov 7, 2022). <br /> <br /> 13 Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3672079 Sandbox Reserved 1732 2022-11-28T12:51:52Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> =='''Insulin Receptor'''==<br /> <Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' /><br /> <scene name='91/919041/Insulin_Receptor/1'></scene><br /> <br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> <br /> == Disease ==<br /> Diseases that involve insulin receptors are normally due to wrong signaling. Insulin regulates blood glucose levels, and with no regulation, it will lead to diseases such as obesity, type I and type II diabetes. Diabetes mainly happens due to elevated levels of blood glucose levels which can result in serious complications over time if not treated correctly. Insulin receptors will interact with cell surface insulin as a mediator of signaling. Around 10.5% of the US population have diabetes. Most of them have type II diabetes. This type of diabetes is considerably more dangerous as it has to do with lifestyle and not the disease coming from a genetic condition that shows up early in life. People with type II diabetes are more susceptive to being obese due to their lifestyle. <br /> <br /> == Relevance ==<br /> Insulin secretion and binding to the insulin receptor initiates a robust physiological response in a healthy individual. The correct insulin signaling is important as it regulates many things that include glucose, lipid, and energy homeostasis. Diseases that happen relating to insulin are due to wrong signaling. These include type I diabetes and type II diabetes. Type I diabetes is normally associated with a genetic condition that shows up early in life. Type II diabetes is normally due to a certain unhealthy lifestyle and will develop over time. <br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. Site L1' is dark green, CR' is orange, L2' is light blue, L2 is yellow, CR is red, L1 is dark blue, β-subunits are brown and light pink, insulin bound to the receptor is hot pink.<ref>http://biorxiv.org/</ref> <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.The beta subunits consist of Fibronectin domain III-2 (FnIII-2) and Fibronectin domain III-3 (FnIII-3). <br /> <br /> [[Image:biochemIBSpt2.png]]<br /> <br /> There are two main conformations of full-length insulin receptors, U-shaped and T-shaped. The U-shaped conformation exists when there is an absence of insulin on the protein, whereas the T-shaped and II-shaped conformations exist in the presence of insulin. The U-shaped conformation is also known as the auto-inhibited state. In this state, the L1 domain contacts the L1’ and L2’ domains of the partnering protein. When insulin binds to the receptor protein, it causes a conformational change from the U-shape to the T-shape conformation. <br /> <br /> == References ==<br /> <br /> 1 Boucher, Jérémie. Kleinridders, André. Kahn1, C. Ronald. Insulin Receptor Signaling in Normal and Insulin-Resistant States. https://cshperspectives.cshlp.org/content/6/1/a009191 (accessed Nov 14, 2022).<br /> <br /> 2 Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 3 Goodsell, D. PDB101: Molecule of the month: Insulin receptor. https://pdb101.rcsb.org/motm/182 (accessed Nov 7, 2022). <br /> <br /> Home - PMC - NCBI https://www.ncbi.nlm.nih.gov/pmc/ (accessed Oct 21, 2022). <br /> <br /> 4 Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 5 Kasago, Masuta. Hedo, Jose A. Yamada, Kenneth M. Kahn, C. Ronald. The Structure of Insulin Receptor and Its Subunits. https://www.jbc.org/article/S0021-9258(18)34032-8/pdf (accessed Oct 21, 2022).<br /> <br /> 6 Lawrence, M. C. Understanding insulin and its receptor from their three-dimensional structures https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513149/#bib1 (accessed Oct 21, 2022). <br /> <br /> 7 Lee, J. and Pilch, P. F. The insulin receptor: structure, function, and signaling. https://journals.physiology.org/doi/abs/10.1152/ajpcell.1994.266.2.c319 (accessed Oct 21, 2022). <br /> <br /> 8 Lee, Yong Hee and Morris F. White. Insulin Receptor Substrate Proteins and Diabetes. https://link.springer.com/content/pdf/10.1007/BF02980074.pdf (accessed Nov 14, 2022)<br /> <br /> 9 PDB101: Global health: Diabetes mellitus: Drugs: Insulin: Insulin receptor https://pdb101.rcsb.org/global-health/diabetes-mellitus/drugs/insulin/insulin-receptor#:~:text=Insulin%20receptors%20are%20proteins%20found,metabolic%20and%20growth%2Drelated%20functions. (accessed Oct 21, 2022). <br /> <br /> 10 PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 11 PF;, L.J.P. (no date) The insulin receptor: Structure, function, and signaling, The American journal of physiology. U.S. National Library of Medicine. Available at: https://pubmed.ncbi.nlm.nih.gov/8141246/ (Accessed: October 21, 2022). <br /> <br /> 12 Scapin, G.; Dandey, V. P.; Zhang, Z.; Prosise, W.; Hruza, A.; Kelly, T.; Mayhood, T.; Strickland, C.; Potter, C. S.; Carragher, B. Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis. https://www.nature.com/articles/nature26153 (accessed Nov 7, 2022). <br /> <br /> 13 Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3671947 Sandbox Reserved 1732 2022-11-27T22:19:31Z

<p>Mary Lively: Undo revision 3671946 by Mary Lively (Talk)</p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> =='''Insulin Receptor'''==<br /> <Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' /><br /> <scene name='91/919041/Insulin_Receptor/1'></scene><br /> <br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> <br /> == Disease ==<br /> Diseases that involve insulin receptors are normally due to wrong signaling. Insulin regulates blood glucose levels, and with no regulation, it will lead to diseases such as obesity, type I and type II diabetes. Diabetes mainly happens due to elevated levels of blood glucose levels which can result in serious complications over time if not treated correctly. Insulin receptors will interact with cell surface insulin as a mediator of signaling. Around 10.5% of the US population have diabetes. Most of them have type II diabetes. This type of diabetes is considerably more dangerous as it has to do with lifestyle and not the disease coming from a genetic condition that shows up early in life. People with type II diabetes are more susceptive to being obese due to their lifestyle. <br /> <br /> == Relevance ==<br /> Insulin secretion and binding to the insulin receptor initiates a robust physiological response in a healthy individual. The correct insulin signaling is important as it regulates many things that include glucose, lipid, and energy homeostasis. Diseases that happen relating to insulin are due to wrong signaling. These include type I diabetes and type II diabetes. Type I diabetes is normally associated with a genetic condition that shows up early in life. Type II diabetes is normally due to a certain unhealthy lifestyle and will develop over time. <br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains.<ref>http://biorxiv.org/</ref> <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.The beta subunits consist of Fibronectin domain III-2 (FnIII-2) and Fibronectin domain III-3 (FnIII-3). <br /> <br /> [[Image:biochemIBSpt2.png]]<br /> <br /> There are two main conformations of full-length insulin receptors, U-shaped and T-shaped. The U-shaped conformation exists when there is an absence of insulin on the protein, whereas the T-shaped and II-shaped conformations exist in the presence of insulin. The U-shaped conformation is also known as the auto-inhibited state. In this state, the L1 domain contacts the L1’ and L2’ domains of the partnering protein. When insulin binds to the receptor protein, it causes a conformational change from the U-shape to the T-shape conformation. <br /> <br /> == References ==<br /> <br /> 1 Boucher, Jérémie. Kleinridders, André. Kahn1, C. Ronald. Insulin Receptor Signaling in Normal and Insulin-Resistant States. https://cshperspectives.cshlp.org/content/6/1/a009191 (accessed Nov 14, 2022).<br /> <br /> 2 Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 3 Goodsell, D. PDB101: Molecule of the month: Insulin receptor. https://pdb101.rcsb.org/motm/182 (accessed Nov 7, 2022). <br /> <br /> Home - PMC - NCBI https://www.ncbi.nlm.nih.gov/pmc/ (accessed Oct 21, 2022). <br /> <br /> 4 Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 5 Kasago, Masuta. Hedo, Jose A. Yamada, Kenneth M. Kahn, C. Ronald. The Structure of Insulin Receptor and Its Subunits. https://www.jbc.org/article/S0021-9258(18)34032-8/pdf (accessed Oct 21, 2022).<br /> <br /> 6 Lawrence, M. C. Understanding insulin and its receptor from their three-dimensional structures https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513149/#bib1 (accessed Oct 21, 2022). <br /> <br /> 7 Lee, J. and Pilch, P. F. The insulin receptor: structure, function, and signaling. https://journals.physiology.org/doi/abs/10.1152/ajpcell.1994.266.2.c319 (accessed Oct 21, 2022). <br /> <br /> 8 Lee, Yong Hee and Morris F. White. Insulin Receptor Substrate Proteins and Diabetes. https://link.springer.com/content/pdf/10.1007/BF02980074.pdf (accessed Nov 14, 2022)<br /> <br /> 9 PDB101: Global health: Diabetes mellitus: Drugs: Insulin: Insulin receptor https://pdb101.rcsb.org/global-health/diabetes-mellitus/drugs/insulin/insulin-receptor#:~:text=Insulin%20receptors%20are%20proteins%20found,metabolic%20and%20growth%2Drelated%20functions. (accessed Oct 21, 2022). <br /> <br /> 10 PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 11 PF;, L.J.P. (no date) The insulin receptor: Structure, function, and signaling, The American journal of physiology. U.S. National Library of Medicine. Available at: https://pubmed.ncbi.nlm.nih.gov/8141246/ (Accessed: October 21, 2022). <br /> <br /> 12 Scapin, G.; Dandey, V. P.; Zhang, Z.; Prosise, W.; Hruza, A.; Kelly, T.; Mayhood, T.; Strickland, C.; Potter, C. S.; Carragher, B. Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis. https://www.nature.com/articles/nature26153 (accessed Nov 7, 2022). <br /> <br /> 13 Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3671946 Sandbox Reserved 1732 2022-11-27T22:18:23Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> =='''Insulin Receptor'''==<br /> <Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' /><br /> <scene name='91/919041/Insulin_Receptor/1'></scene><br /> <br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> <br /> == Disease ==<br /> Diseases that involve insulin receptors are normally due to wrong signaling. Insulin regulates blood glucose levels, and with no regulation, it will lead to diseases such as obesity, type I and type II diabetes. Diabetes mainly happens due to elevated levels of blood glucose levels which can result in serious complications over time if not treated correctly. Insulin receptors will interact with cell surface insulin as a mediator of signaling. Around 10.5% of the US population have diabetes. Most of them have type II diabetes. This type of diabetes is considerably more dangerous as it has to do with lifestyle and not the disease coming from a genetic condition that shows up early in life. People with type II diabetes are more susceptive to being obese due to their lifestyle. <br /> <br /> == Relevance ==<br /> Insulin secretion and binding to the insulin receptor initiates a robust physiological response in a healthy individual. The correct insulin signaling is important as it regulates many things that include glucose, lipid, and energy homeostasis. Diseases that happen relating to insulin are due to wrong signaling. These include type I diabetes and type II diabetes. Type I diabetes is normally associated with a genetic condition that shows up early in life. Type II diabetes is normally due to a certain unhealthy lifestyle and will develop over time. <br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains.<ref>http://biorxiv.org/<ref> <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.The beta subunits consist of Fibronectin domain III-2 (FnIII-2) and Fibronectin domain III-3 (FnIII-3). <br /> <br /> [[Image:biochemIBSpt2.png]]<br /> <br /> There are two main conformations of full-length insulin receptors, U-shaped and T-shaped. The U-shaped conformation exists when there is an absence of insulin on the protein, whereas the T-shaped and II-shaped conformations exist in the presence of insulin. The U-shaped conformation is also known as the auto-inhibited state. In this state, the L1 domain contacts the L1’ and L2’ domains of the partnering protein. When insulin binds to the receptor protein, it causes a conformational change from the U-shape to the T-shape conformation. <br /> <br /> == References ==<br /> <br /> 1 Boucher, Jérémie. Kleinridders, André. Kahn1, C. Ronald. Insulin Receptor Signaling in Normal and Insulin-Resistant States. https://cshperspectives.cshlp.org/content/6/1/a009191 (accessed Nov 14, 2022).<br /> <br /> 2 Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 3 Goodsell, D. PDB101: Molecule of the month: Insulin receptor. https://pdb101.rcsb.org/motm/182 (accessed Nov 7, 2022). <br /> <br /> Home - PMC - NCBI https://www.ncbi.nlm.nih.gov/pmc/ (accessed Oct 21, 2022). <br /> <br /> 4 Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 5 Kasago, Masuta. Hedo, Jose A. Yamada, Kenneth M. Kahn, C. Ronald. The Structure of Insulin Receptor and Its Subunits. https://www.jbc.org/article/S0021-9258(18)34032-8/pdf (accessed Oct 21, 2022).<br /> <br /> 6 Lawrence, M. C. Understanding insulin and its receptor from their three-dimensional structures https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513149/#bib1 (accessed Oct 21, 2022). <br /> <br /> 7 Lee, J. and Pilch, P. F. The insulin receptor: structure, function, and signaling. https://journals.physiology.org/doi/abs/10.1152/ajpcell.1994.266.2.c319 (accessed Oct 21, 2022). <br /> <br /> 8 Lee, Yong Hee and Morris F. White. Insulin Receptor Substrate Proteins and Diabetes. https://link.springer.com/content/pdf/10.1007/BF02980074.pdf (accessed Nov 14, 2022)<br /> <br /> 9 PDB101: Global health: Diabetes mellitus: Drugs: Insulin: Insulin receptor https://pdb101.rcsb.org/global-health/diabetes-mellitus/drugs/insulin/insulin-receptor#:~:text=Insulin%20receptors%20are%20proteins%20found,metabolic%20and%20growth%2Drelated%20functions. (accessed Oct 21, 2022). <br /> <br /> 10 PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 11 PF;, L.J.P. (no date) The insulin receptor: Structure, function, and signaling, The American journal of physiology. U.S. National Library of Medicine. Available at: https://pubmed.ncbi.nlm.nih.gov/8141246/ (Accessed: October 21, 2022). <br /> <br /> 12 Scapin, G.; Dandey, V. P.; Zhang, Z.; Prosise, W.; Hruza, A.; Kelly, T.; Mayhood, T.; Strickland, C.; Potter, C. S.; Carragher, B. Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis. https://www.nature.com/articles/nature26153 (accessed Nov 7, 2022). <br /> <br /> 13 Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3671945 Sandbox Reserved 1732 2022-11-27T22:14:44Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> =='''Insulin Receptor'''==<br /> <Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' /><br /> <scene name='91/919041/Insulin_Receptor/1'></scene><br /> <br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> <br /> == Disease ==<br /> Diseases that involve insulin receptors are normally due to wrong signaling. Insulin regulates blood glucose levels, and with no regulation, it will lead to diseases such as obesity, type I and type II diabetes. Diabetes mainly happens due to elevated levels of blood glucose levels which can result in serious complications over time if not treated correctly. Insulin receptors will interact with cell surface insulin as a mediator of signaling. Around 10.5% of the US population have diabetes. Most of them have type II diabetes. This type of diabetes is considerably more dangerous as it has to do with lifestyle and not the disease coming from a genetic condition that shows up early in life. People with type II diabetes are more susceptive to being obese due to their lifestyle. <br /> <br /> == Relevance ==<br /> Insulin secretion and binding to the insulin receptor initiates a robust physiological response in a healthy individual. The correct insulin signaling is important as it regulates many things that include glucose, lipid, and energy homeostasis. Diseases that happen relating to insulin are due to wrong signaling. These include type I diabetes and type II diabetes. Type I diabetes is normally associated with a genetic condition that shows up early in life. Type II diabetes is normally due to a certain unhealthy lifestyle and will develop over time. <br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains.<ref>http://biorxiv.org/</ref> <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.The beta subunits consist of Fibronectin domain III-2 (FnIII-2) and Fibronectin domain III-3 (FnIII-3). <br /> <br /> [[Image:biochemIBSpt2.png]]<br /> <br /> There are two main conformations of full-length insulin receptors, U-shaped and T-shaped. The U-shaped conformation exists when there is an absence of insulin on the protein, whereas the T-shaped and II-shaped conformations exist in the presence of insulin. The U-shaped conformation is also known as the auto-inhibited state. In this state, the L1 domain contacts the L1’ and L2’ domains of the partnering protein. When insulin binds to the receptor protein, it causes a conformational change from the U-shape to the T-shape conformation. <br /> <br /> == References ==<br /> <br /> 1 Boucher, Jérémie. Kleinridders, André. Kahn1, C. Ronald. Insulin Receptor Signaling in Normal and Insulin-Resistant States. https://cshperspectives.cshlp.org/content/6/1/a009191 (accessed Nov 14, 2022).<br /> <br /> 2 Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 3 Goodsell, D. PDB101: Molecule of the month: Insulin receptor. https://pdb101.rcsb.org/motm/182 (accessed Nov 7, 2022). <br /> <br /> Home - PMC - NCBI https://www.ncbi.nlm.nih.gov/pmc/ (accessed Oct 21, 2022). <br /> <br /> 4 Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 5 Kasago, Masuta. Hedo, Jose A. Yamada, Kenneth M. Kahn, C. Ronald. The Structure of Insulin Receptor and Its Subunits. https://www.jbc.org/article/S0021-9258(18)34032-8/pdf (accessed Oct 21, 2022).<br /> <br /> 6 Lawrence, M. C. Understanding insulin and its receptor from their three-dimensional structures https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8513149/#bib1 (accessed Oct 21, 2022). <br /> <br /> 7 Lee, J. and Pilch, P. F. The insulin receptor: structure, function, and signaling. https://journals.physiology.org/doi/abs/10.1152/ajpcell.1994.266.2.c319 (accessed Oct 21, 2022). <br /> <br /> 8 Lee, Yong Hee and Morris F. White. Insulin Receptor Substrate Proteins and Diabetes. https://link.springer.com/content/pdf/10.1007/BF02980074.pdf (accessed Nov 14, 2022)<br /> <br /> 9 PDB101: Global health: Diabetes mellitus: Drugs: Insulin: Insulin receptor https://pdb101.rcsb.org/global-health/diabetes-mellitus/drugs/insulin/insulin-receptor#:~:text=Insulin%20receptors%20are%20proteins%20found,metabolic%20and%20growth%2Drelated%20functions. (accessed Oct 21, 2022). <br /> <br /> 10 PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 11 PF;, L.J.P. (no date) The insulin receptor: Structure, function, and signaling, The American journal of physiology. U.S. National Library of Medicine. Available at: https://pubmed.ncbi.nlm.nih.gov/8141246/ (Accessed: October 21, 2022). <br /> <br /> 12 Scapin, G.; Dandey, V. P.; Zhang, Z.; Prosise, W.; Hruza, A.; Kelly, T.; Mayhood, T.; Strickland, C.; Potter, C. S.; Carragher, B. Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis. https://www.nature.com/articles/nature26153 (accessed Nov 7, 2022). <br /> <br /> 13 Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663175 Sandbox Reserved 1732 2022-11-14T23:30:05Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Insulin Receptor Protein==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.The beta subunits consist of Fibronectin domain III-2 (FnIII-2) and Fibronectin domain III-3 (FnIII-3). <br /> <br /> [[Image:biochemIBSpt2.png]]<br /> <br /> There are two main conformations of full-length insulin receptors, U-shaped and T-shaped. The U-shaped conformation exists when there is an absence of insulin on the protein, whereas the T-shaped and II-shaped conformations exist in the presence of insulin. The U-shaped conformation is also known as the auto-inhibited state. In this state, the L1 domain contacts the L1’ and L2’ domains of the partnering protein. When insulin binds to the receptor protein, it causes a conformational change from the U-shape to the T-shape conformation. <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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663143 Sandbox Reserved 1732 2022-11-14T18:39:13Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Insulin Receptor Protein==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly. <br /> <br /> [[Image:biochemIBSpt2.png]]<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663142 Sandbox Reserved 1732 2022-11-14T18:38:38Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. <br /> <br /> [[Image:6CE7.png]]<br /> <br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly. <br /> <br /> [[Image:biochemIBSpt2.png]]<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=File:BiochemIBSpt2.png&diff=3663141 File:BiochemIBSpt2.png 2022-11-14T18:38:07Z

<p>Mary Lively: Sites 1 and 1' are green. Sites 2 and 2' are red.</p> <hr /> <div>Sites 1 and 1' are green. Sites 2 and 2' are red.</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663140 Sandbox Reserved 1732 2022-11-14T18:37:26Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. <br /> [[Image:6CE7.png]]<br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly. <br /> [[Image:biochemIBSpt2.png]]<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=File:BiochemIBS.png&diff=3663139 File:BiochemIBS.png 2022-11-14T18:35:23Z

<p>Mary Lively: Sites 1 and 1' are green. Sites 2 and 2' are red.</p> <hr /> <div>Sites 1 and 1' are green. Sites 2 and 2' are red.</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663138 Sandbox Reserved 1732 2022-11-14T18:34:40Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. <br /> [[Image:6CE7.png]]<br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly. <br /> [[Image:biochemIBS.png]]<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663137 Sandbox Reserved 1732 2022-11-14T18:33:14Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. <br /> [[Image:6CE7.png]]<br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly. <br /> [[Image:binding.png]]<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=File:6CE7.png&diff=3663136 File:6CE7.png 2022-11-14T18:31:25Z

<p>Mary Lively: Site L1' is dark green, CR' is orange, L2' is light blue, L2 is yellow, CR is red, L1 is dark blue, β-subunits are brown and light pink, insulin bound to the receptor is hot pink.</p> <hr /> <div>Site L1' is dark green, CR' is orange, L2' is light blue, L2 is yellow, CR is red, L1 is dark blue, β-subunits are brown and light pink, insulin bound to the receptor is hot pink.</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663135 Sandbox Reserved 1732 2022-11-14T18:28:21Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains. <br /> [[Image:6CE7.png]]<br /> Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly. <br /> <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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663134 Sandbox Reserved 1732 2022-11-14T18:05:10Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain. <br /> The extracellular domain has a quaternary organization. <br /> When insulin binds to the insulin receptor, transmembrane signaling and autophosphorylation of the β-chains at multiple sites is triggered. <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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663105 Sandbox Reserved 1732 2022-11-14T00:15:36Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels <ref>PMID:PDB101</ref>.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663104 Sandbox Reserved 1732 2022-11-14T00:09:40Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663103 Sandbox Reserved 1732 2022-11-13T23:59:38Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> In order to fully comprehend insulin receptors, it is important to understand what insulin is. Insulin is a hormone that allows our bodies to absorb glucose that is found in our bloodstream. The main source of insulin in the body is from the pancreas, which consists of islets. Islets are what produce and determine the amount of insulin based on the body's blood glucose levels. The higher the glucose levels, the more insulin is produced and released in order to bring blood sugar levels back to an equilibrium. <br /> == Disease ==<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3662898 Sandbox Reserved 1732 2022-11-09T21:46:05Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels.<br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> <br /> == Disease ==<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3662897 Sandbox Reserved 1732 2022-11-09T21:45:21Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels.^[1] <br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> <br /> == Disease ==<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3662896 Sandbox Reserved 1732 2022-11-09T21:42:24Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels. <br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> <br /> == Disease ==<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 /> <br /> 1. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3662895 Sandbox Reserved 1732 2022-11-09T21:38:37Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels. <br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> <br /> == Disease ==<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 /> <br /> [1]. PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022).</div>

Mary Lively https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3662894 Sandbox Reserved 1732 2022-11-09T21:36:37Z

<p>Mary Lively: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == What is an Insulin Receptor? ==<br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. When insulin binds to the receptor, it is activated and triggers a series of chemical reactions within the cell. These reactions cause an uptake in glucose and other metabolic and growth-related functions. The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulin which allows people with diabetes to maintain the blood sugar levels necessary. Along with controlling homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels. <br /> <br /> == Function ==<br /> Insulin receptors are regions outside of a cell that allow the cell to bind with the insulin in the bloodstream. The main physiological role of insulin receptors is metabolic regulation. <br /> <br /> In order for the receptors to properly interact with Insulin, Insulin must undergo a conformational change. This conformational change is when the C- terminal of the B chain must disengage from the hormone's core. Now the Insulin can properly bind to the appropriate receptor. <br /> <br /> == Insulin == <br /> <br /> == Disease ==<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>

Mary Lively