Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Kiana+Aneli Proteopedia - User contributions [en] 2026-10-04T19:52:02Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663274 Sandbox Reserved 1740 2022-11-15T11:52:23Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell, as well as the containment of water within the cell. <br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose. Cellulose is a polymer that is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on the synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> The primary structure of cellulose sythase is a long chain of glucose units. It is attached through Beta(1,4) linkages which appear to be like a sheet. <br /> Beta linkages form Beta sheets, 6 stranded beta sheets to be exact along with the beta sheets there can be found the 5 alpha helices. These chains form hydrogen bonds with each other forming microfibrils helping to create the overall strength and stability of cellulose. Though much research has been done, the tertiary structure of cellulose synthase has been difficult to find because of complications with things like purification of the active enzyme, and the overall difficulty of crystalizing plant cellulose synthase.<br /> <br /> == References ==<br /> Abidi, Wiem. Torres-Sánchez, Lucía. Siroy, Axel. Krasteva, Petya Violinova. Weaving of bacterial cellulose by the Bcs secretion systems. https://doi.org/10.1093/femsre/fuab051 (accessed Oct 21, 2022).<br /> <br /> Carroll, A.; Specht, C. D. Understanding Plant Cellulose Synthases through a Comprehensive Investigation of the Cellulose Synthase Family Sequences. https://doi.org/10.3389/fpls.2011.00005. (accessed Oct 21, 2022)<br /> <br /> Duan, P. Wei, M. Zhang, R. et al. Identification and bioinformatic analysis of the CaCesA/Csls family members and the expression of the CaCslD1 in the flower buds of CMS/Rf system in pepper. https://doi.org/10.1007/s10142-022-00896-y (accessed Oct 21, 2022).<br /> <br /> Kondo, T. Nakamura, Y. Nojima, S. Yao, M. Imai, T. The BcsD subunit of type I bacterial cellulose synthase interacts dynamically with the BcsAB catalytic core complex. https://doi.org/10.1002/1873-3468.14495 (accessed Oct 21, 2022).<br /> <br /> Philos Trans A Math Phys Eng Sci. 10.1098/rsta.2017.0048 (accessed Oct 21, 2022)<br /> <br /> Xue, Jan. Purushotham, Pallinti. Acheson, Justin F. Ho, Ruoya. Zimmer, Jochen. McFarlane, Ciaran. Petegem, Filip Van. Martone, Patrick T. Samuels, A Lacey. Functional characterization of a cellulose synthase. https://doi.org/10.1093/jxb/erab414 (accessed Oct 21, 2022)<br /> <br /> Zhu, Yu. McFarlane Heather E. Regulation of cellulose synthesis via exocytosis and endocytosis. (accessed Oct 21, 2022)</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663273 Sandbox Reserved 1740 2022-11-15T11:49:13Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell, as well as the containment of water within the cell. <br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose. Cellulose is a polymer that is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on the synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> The primary structure is a long chain of glucose units. It is attached through Beta(1,4) linkages which appear to be like a sheet. <br /> Beta linkages form Beta sheets, 6 stranded beta sheets to be exact as well as 5 alpha helices. These chains form hydrogen bonds with each other forming microfibrils helping to create the overall strength and stability of cellulose. Though much research has been done, the tertiary structure of cellulose synthase has been difficult to find because of complications with things like purification of the active enzyme, and the overall difficulty of crystalizing plant cellulose synthase.<br /> <br /> == References ==<br /> Abidi, Wiem. Torres-Sánchez, Lucía. Siroy, Axel. Krasteva, Petya Violinova. Weaving of bacterial cellulose by the Bcs secretion systems. https://doi.org/10.1093/femsre/fuab051 (accessed Oct 21, 2022).<br /> <br /> Carroll, A.; Specht, C. D. Understanding Plant Cellulose Synthases through a Comprehensive Investigation of the Cellulose Synthase Family Sequences. https://doi.org/10.3389/fpls.2011.00005. (accessed Oct 21, 2022)<br /> <br /> Duan, P. Wei, M. Zhang, R. et al. Identification and bioinformatic analysis of the CaCesA/Csls family members and the expression of the CaCslD1 in the flower buds of CMS/Rf system in pepper. https://doi.org/10.1007/s10142-022-00896-y (accessed Oct 21, 2022).<br /> <br /> Kondo, T. Nakamura, Y. Nojima, S. Yao, M. Imai, T. The BcsD subunit of type I bacterial cellulose synthase interacts dynamically with the BcsAB catalytic core complex. https://doi.org/10.1002/1873-3468.14495 (accessed Oct 21, 2022).<br /> <br /> Philos Trans A Math Phys Eng Sci. 10.1098/rsta.2017.0048 (accessed Oct 21, 2022)<br /> <br /> Xue, Jan. Purushotham, Pallinti. Acheson, Justin F. Ho, Ruoya. Zimmer, Jochen. McFarlane, Ciaran. Petegem, Filip Van. Martone, Patrick T. Samuels, A Lacey. Functional characterization of a cellulose synthase. https://doi.org/10.1093/jxb/erab414 (accessed Oct 21, 2022)<br /> <br /> Zhu, Yu. McFarlane Heather E. Regulation of cellulose synthesis via exocytosis and endocytosis. (accessed Oct 21, 2022)</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663271 Sandbox Reserved 1740 2022-11-15T11:48:03Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell , as well as the containment of water within the cell. <br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose . Cellulose is a polymer which is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on they synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> The primary structure is a long chain of glucose units. It is attached through Beta(1,4) linkages which appear to be like a sheet. <br /> Beta linkages form Beta sheets, 6 stranded beta sheets to be exact as well as 5 alpha helices. These chains form hydrogen bonds with each other forming microfibrils helping to create the overall strength and stability of cellulose. Though much research has been done, the tertiary structure of cellulose synthase has been difficult to find because of complications with things like purification of the active enzyme, and the overall difficulty of crystalizing plant cellulose synthase.<br /> <br /> == References ==<br /> Abidi, Wiem. Torres-Sánchez, Lucía. Siroy, Axel. Krasteva, Petya Violinova. Weaving of bacterial cellulose by the Bcs secretion systems. https://doi.org/10.1093/femsre/fuab051 (accessed Oct 21, 2022).<br /> <br /> Carroll, A.; Specht, C. D. Understanding Plant Cellulose Synthases through a Comprehensive Investigation of the Cellulose Synthase Family Sequences. https://doi.org/10.3389/fpls.2011.00005. (accessed Oct 21, 2022)<br /> <br /> Duan, P. Wei, M. Zhang, R. et al. Identification and bioinformatic analysis of the CaCesA/Csls family members and the expression of the CaCslD1 in the flower buds of CMS/Rf system in pepper. https://doi.org/10.1007/s10142-022-00896-y (accessed Oct 21, 2022).<br /> <br /> Kondo, T. Nakamura, Y. Nojima, S. Yao, M. Imai, T. The BcsD subunit of type I bacterial cellulose synthase interacts dynamically with the BcsAB catalytic core complex. https://doi.org/10.1002/1873-3468.14495 (accessed Oct 21, 2022).<br /> <br /> Philos Trans A Math Phys Eng Sci. 10.1098/rsta.2017.0048 (accessed Oct 21, 2022)<br /> <br /> Xue, Jan. Purushotham, Pallinti. Acheson, Justin F. Ho, Ruoya. Zimmer, Jochen. McFarlane, Ciaran. Petegem, Filip Van. Martone, Patrick T. Samuels, A Lacey. Functional characterization of a cellulose synthase. https://doi.org/10.1093/jxb/erab414 (accessed Oct 21, 2022)<br /> <br /> Zhu, Yu. McFarlane Heather E. Regulation of cellulose synthesis via exocytosis and endocytosis. (accessed Oct 21, 2022)</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663264 Sandbox Reserved 1740 2022-11-15T11:20:23Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell , as well as the containment of water within the cell. <br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose . Cellulose is a polymer which is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on they synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> <br /> == References ==<br /> Abidi, Wiem. Torres-Sánchez, Lucía. Siroy, Axel. Krasteva, Petya Violinova. Weaving of bacterial cellulose by the Bcs secretion systems. https://doi.org/10.1093/femsre/fuab051 (accessed Oct 21, 2022).<br /> <br /> Carroll, A.; Specht, C. D. Understanding Plant Cellulose Synthases through a Comprehensive Investigation of the Cellulose Synthase Family Sequences. https://doi.org/10.3389/fpls.2011.00005. (accessed Oct 21, 2022)<br /> <br /> Duan, P. Wei, M. Zhang, R. et al. Identification and bioinformatic analysis of the CaCesA/Csls family members and the expression of the CaCslD1 in the flower buds of CMS/Rf system in pepper. https://doi.org/10.1007/s10142-022-00896-y (accessed Oct 21, 2022).<br /> <br /> Kondo, T. Nakamura, Y. Nojima, S. Yao, M. Imai, T. The BcsD subunit of type I bacterial cellulose synthase interacts dynamically with the BcsAB catalytic core complex. https://doi.org/10.1002/1873-3468.14495 (accessed Oct 21, 2022).<br /> <br /> Philos Trans A Math Phys Eng Sci. 10.1098/rsta.2017.0048 (accessed Oct 21, 2022)<br /> <br /> Xue, Jan. Purushotham, Pallinti. Acheson, Justin F. Ho, Ruoya. Zimmer, Jochen. McFarlane, Ciaran. Petegem, Filip Van. Martone, Patrick T. Samuels, A Lacey. Functional characterization of a cellulose synthase. https://doi.org/10.1093/jxb/erab414 (accessed Oct 21, 2022)<br /> <br /> Zhu, Yu. McFarlane Heather E. Regulation of cellulose synthesis via exocytosis and endocytosis. (accessed Oct 21, 2022)</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663259 Sandbox Reserved 1740 2022-11-15T10:37:03Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell , as well as the containment of water within the cell. <br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose . Cellulose is a polymer which is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on they synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> <br /> == References ==<br /> <references/></div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663258 Sandbox Reserved 1740 2022-11-15T10:36:31Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell , as well as the containment of water within the cell. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose . Cellulose is a polymer which is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on they synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> <br /> == References ==<br /> <references/></div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663257 Sandbox Reserved 1740 2022-11-15T10:35:57Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell , as well as the containment of water within the cell. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose . Cellulose is a polymer which is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on they synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><br /> == References ==<br /> <references/></div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663256 Sandbox Reserved 1740 2022-11-15T10:34:57Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell , as well as the containment of water within the cell. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose . Cellulose is a polymer which is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on they synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><br /> <br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><br /> == References ==<br /> <references/></div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1740&diff=3663255 Sandbox Reserved 1740 2022-11-15T10:31:49Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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 /> == Function ==<br /> Cellulose synthase has two main jobs. The first of these two being the synthesis or creation of the polysaccharide cellulose and the second job of cellulose synthase is to create the crystalline microfibril structure. Cellulose is one of the main components in the cell wall and is responsible for protecting the cell from unwarranted pathogens that might try and harm the cell. The overall shape and form of the cell , as well as the containment of water within the cell. <br /> == Disease ==<br /> <br /> == Relevance ==<br /> Why is cellulose synthase so important? Cellular synthase is an enzyme that helps form the structure of cellulose . Cellulose is a polymer which is composed of many other homopolymers. Cellulose has many important jobs within a cell that without cellulose the cell could not function. Things like the formation of the cell wall which is vital to the life of a plant cell are all dependent on they synthesis of cellulose.<br /> <br /> == Structural highlights ==<br /> <applet load='4HG6' size'400' frame='true' align='right' caption='this is my caption' /><br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663252 Sandbox Reserved 1732 2022-11-15T09:55:54Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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'>Text To Be Displayed</scene><br /> <br /> <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. <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 /> 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 /> Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 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 /> Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 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 /> 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 /> 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 /> 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 /> 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 /> PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 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 /> 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 /> Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663228 Sandbox Reserved 1732 2022-11-15T05:55:54Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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'>Text To Be Displayed</scene><br /> <br /> <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. <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 /> 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 /> Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 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 /> Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 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 /> 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 /> 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 /> 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 /> 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 /> PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 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 /> 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 /> Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663227 Sandbox Reserved 1732 2022-11-15T05:52:01Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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'>Text To Be Displayed</scene><br /> <br /> <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. <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 /> 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 /> Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 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 /> Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 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 /> 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 /> 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 /> 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 /> PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 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 /> 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 /> Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663217 Sandbox Reserved 1732 2022-11-15T04:42:26Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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'>Text To Be Displayed</scene><br /> <br /> <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 /> == Disease ==<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. <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 /> 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 /> Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 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 /> Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 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 /> 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 /> 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 /> 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 /> PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 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 /> 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 /> Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663215 Sandbox Reserved 1732 2022-11-15T04:35:51Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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'>Text To Be Displayed</scene><br /> <br /> <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 /> == Disease ==<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. <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 /> 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 /> Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 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 /> Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022).<br /> <br /> 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 /> 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 /> 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 /> 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 /> PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 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 /> 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 /> Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3663213 Sandbox Reserved 1732 2022-11-15T04:09:53Z

<p>Kiana Aneli: </p> <hr /> <div>{{Sandbox_Reserved_Kim_Lane}}<br /> <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'>Text To Be Displayed</scene><br /> <br /> <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 /> == Disease ==<br /> <br /> == Relevance ==<br /> Insulin secretion and binding to the insulin receptor initiates a robust physiological response in a healthy individual. 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 /> == 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 /> <br /> Felman, A.; Prelipcean, M. Insulin: Function and types. https://www.medicalnewstoday.com/articles/323760 (accessed Nov 1, 2022). <br /> <br /> 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 /> Hubbard, Stevan R. Wei, Lei. Ellis, Leland. Hendrickson, Wayne A. https://www.nature.com/articles/372746a0 (accessed Oct 21, 2022) <br /> <br /> 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 /> 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 /> 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 /> 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 /> PDB101: Molecule of the month: Insulin receptor https://pdb101.rcsb.org/motm/182 (accessed Oct 21, 2022). <br /> <br /> 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 /> 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 /> Yang, Y. X.; Li, P.; Wang, P.; Ting Zhu, B. BioRxiv. http://biorxiv.org/ (accessed Nov 14, 2022).</div>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3658532 Sandbox Reserved 1732 2022-11-07T13:23:56Z

<p>Kiana Aneli: </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 /> == 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>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3658530 Sandbox Reserved 1732 2022-11-07T13:16:59Z

<p>Kiana Aneli: </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 /> == 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 /> == 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>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3658529 Sandbox Reserved 1732 2022-11-07T13:16:34Z

<p>Kiana Aneli: </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 /> == 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 /> == idk ==<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>

Kiana Aneli https://proteopedia.org/index.php?title=Sandbox_Reserved_1732&diff=3658528 Sandbox Reserved 1732 2022-11-07T13:16:11Z

<p>Kiana Aneli: </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 /> == 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 /> == 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>

Kiana Aneli https://proteopedia.org/index.php?title=Help_talk:Getting_Started_in_Proteopedia&diff=3658527 Help talk:Getting Started in Proteopedia 2022-11-07T13:12:55Z

<p>Kiana Aneli: </p> <hr /> <div>== Icons in the editor ==<br /> <br /> Here is a cheat sheet for the editor icons:<br /> <br /> [[Image:Proteopedia Editor Icons.JPG]]<br /> <br /> I can't edit the help page, so I posted it here.<br /> <br /> What is an insulin receptor? <br /> <br /> An insulin receptor is a large protein that binds to insulin and passes its message into the cell. <br /> <br /> 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. <br /> <br /> The insulin receptor binds to insulin that is produced in our bodies as well as FDA approved designer insulins which allows people with diabetes to maintain the blood sugar levels necessary. <br /> <br /> Along with controlling glucose homeostasis, insulin receptors also play a crucial role in regulating lipid, protein, and carbohydrate metabolism, as well as modulating brain neurotransmitter levels.</div>

Kiana Aneli