Johnson's Monday Lab Sandbox for Insulin Receptor
From Proteopedia
(Difference between revisions)
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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. | 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. | ||
| - | == | + | ==Function of the Receptor== |
==Insulin== | ==Insulin== | ||
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The insulin receptor is a '''heterotetramer''' which resides in the plasma membrane of '''insulin target cells'''. The ectodomain is made up of two alpha subunits and two beta subunits. Each alpha subunit contains two leucine rich domains and a cysteine rich domain. Each beta subunit is made up of three fibronectin type III domains. The insulin receptor extends intracellularly from the beta subunits of the ectodomain by way of a '''transmembrane''' alpha helix. The intracellular domain contains two tyrosine kinase domains. NEED TO DISCUSS V VS T SHAPE. OVERLAPPING OF HOMODIMERS. C TERM ALPHA HELIX. COVALENT DISULFIDE BONDS | The insulin receptor is a '''heterotetramer''' which resides in the plasma membrane of '''insulin target cells'''. The ectodomain is made up of two alpha subunits and two beta subunits. Each alpha subunit contains two leucine rich domains and a cysteine rich domain. Each beta subunit is made up of three fibronectin type III domains. The insulin receptor extends intracellularly from the beta subunits of the ectodomain by way of a '''transmembrane''' alpha helix. The intracellular domain contains two tyrosine kinase domains. NEED TO DISCUSS V VS T SHAPE. OVERLAPPING OF HOMODIMERS. C TERM ALPHA HELIX. COVALENT DISULFIDE BONDS | ||
| - | === | + | ===Insulin Binding=== |
The insulin receptor unit has four separate sites for the insulin molecule to bind to. There are two pairs of two identical binding sites referred to as 1 and 1' and then 2 and 2'. The insulin molecules bind to these sites mostly through [http://en.wikipedia.org/wiki/Hydrophobic_effect hydrophobic interactions]. Despite a majority of the interactions being similar, sites 1 and 1' have a higher binding affinity than sites 2 and 2' due to site one having a larger surface area (706 square angstroms) exposed for insulin to bind to compared to site 2 (394 square angstroms)<ref name="Uchikawa" />. | The insulin receptor unit has four separate sites for the insulin molecule to bind to. There are two pairs of two identical binding sites referred to as 1 and 1' and then 2 and 2'. The insulin molecules bind to these sites mostly through [http://en.wikipedia.org/wiki/Hydrophobic_effect hydrophobic interactions]. Despite a majority of the interactions being similar, sites 1 and 1' have a higher binding affinity than sites 2 and 2' due to site one having a larger surface area (706 square angstroms) exposed for insulin to bind to compared to site 2 (394 square angstroms)<ref name="Uchikawa" />. | ||
Revision as of 03:12, 23 March 2020
Insulin Receptor
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