Sandbox Reserved 1170
From Proteopedia
(Difference between revisions)
| Line 5: | Line 5: | ||
== Function == | == Function == | ||
| - | Human GPR40 (hGPR40) is a G-protein | + | Human GPR40 (hGPR40) is a G-protein coupled receptor that binds free fatty acids to enhance glucose dependent insulin signaling.<ref name="Srivastava">PMID:25043059</ref> |
== Structure == | == Structure == | ||
Like most G-protein coupled receptors, hGPR40 contains '''seven transmembrane helices'''. In order obtain a crystallized structure of the protein, four <scene name='72/721541/Stabilizing_mutations/3'>stabilizing mutations</scene> (<scene name='72/721541/L42a/2'>L42A</scene>, <scene name='72/721541/F88a/2'>F88A</scene>, <scene name='72/721541/G103a/2'>G103A</scene>, <scene name='72/721541/Y202f/2'>Y202F</scene>) were made to increase expression levels and thermal stability of the protein.<ref name="Srivastava"/> | Like most G-protein coupled receptors, hGPR40 contains '''seven transmembrane helices'''. In order obtain a crystallized structure of the protein, four <scene name='72/721541/Stabilizing_mutations/3'>stabilizing mutations</scene> (<scene name='72/721541/L42a/2'>L42A</scene>, <scene name='72/721541/F88a/2'>F88A</scene>, <scene name='72/721541/G103a/2'>G103A</scene>, <scene name='72/721541/Y202f/2'>Y202F</scene>) were made to increase expression levels and thermal stability of the protein.<ref name="Srivastava"/> | ||
=== Charge Network === | === Charge Network === | ||
| + | hGPR40 has a distinct binding pocket that is established by several key residues. These residues have either a charged or polar R-group that allows them to develop a charge network. | ||
[[Image:charge network residues.png|300 px|right|thumb|Figure Legend]] | [[Image:charge network residues.png|300 px|right|thumb|Figure Legend]] | ||
<scene name='72/721541/Hydrogen_binding_1/3'>Key Binding Residues</scene> | <scene name='72/721541/Hydrogen_binding_1/3'>Key Binding Residues</scene> | ||
Revision as of 18:23, 28 March 2016
Human GPR40
| |||||||||||
References
- ↑ 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
- ↑ 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
- ↑ 3.0 3.1 Srivastava A, Yano J, Hirozane Y, Kefala G, Gruswitz F, Snell G, Lane W, Ivetac A, Aertgeerts K, Nguyen J, Jennings A, Okada K. High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875. Nature. 2014 Jul 20. doi: 10.1038/nature13494. PMID:25043059 doi:http://dx.doi.org/10.1038/nature13494
