Johnson's Monday Lab Sandbox for Insulin Receptor

From Proteopedia

proteopedia linkproteopedia link

Revision as of 21:01, 21 March 2020 (edit) Maxwell Todd (Talk | contribs) ← Previous diff		Revision as of 21:11, 21 March 2020 (edit) (undo) Maxwell Todd (Talk | contribs) Next diff →
Line 11:		Line 11:
	===How Insulin Binds===		===How Insulin Binds===
-		+	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 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">
	</StructureSection>		</StructureSection>

---

Revision as of 21:11, 21 March 2020

Your Heading Here (maybe something like 'Structure')

spinqualitylabelsall models Insulin Receptor with Four Insulin Bound - 6sof Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image This is a default text for your page Johnson's Monday Lab Sandbox for Insulin Receptor. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. Contents 1 Purpose of Receptor 2 Structure 2.1 Conformational Changes 2.2 How Insulin Binds Purpose of Receptor Structure Conformational Changes How Insulin Binds 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 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)[3]

References

^{[3] [4] [5]}

1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
3. ↑ ^{3.0 3.1}
4. ↑ Boucher J, Kleinridders A, Kahn CR. Insulin receptor signaling in normal and insulin-resistant states. Cold Spring Harb Perspect Biol. 2014 Jan 1;6(1). pii: 6/1/a009191. doi:, 10.1101/cshperspect.a009191. PMID:24384568 doi:http://dx.doi.org/10.1101/cshperspect.a009191
5. ↑ De Meyts P. The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling. Diabetologia. 1994 Sep;37 Suppl 2:S135-48. doi: 10.1007/bf00400837. PMID:7821729 doi:http://dx.doi.org/10.1007/bf00400837

Student Contributors

• Maxwell Todd
• Abby Hillan
• Andrew Scheel