Sandbox Reserved 1167

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Revision as of 13:13, 29 March 2016

This Sandbox is Reserved from Jan 11 through August 12, 2016 for use in the course CH462 Central Metabolism taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1160 through Sandbox Reserved 1184.

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This is a default text for your page '. 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.

1 Background
2 Function
3 Structure
- 3.1 Class B Structural Components
- 3.2 Unique components to the GPCR
4 Glucagon Binding
5 Clinical Relevance

Background

The human glucagon receptor is one of 15 secretin-like, or Class B, members of G-protein-coupled receptors (GCPRs). Like other GCPRs, it has a helical domain (shown in blue) and a globular N-terminus extracellular domain (). As its name suggests, the 7tm is made up of alpha helices that pass through the membrane seven times.

During times of fasting (or low blood sugar) the pancreas dispatches glucagon to activate the GCPR in the liver, which causes the release of glucose into the blood.

Secretin-like GPCRs contains both a 7tm domain (blue) and a globular N-terminus ECD (magenta)

The Extracellular Domain has a α-β-β structure which consists of two antiparallel β-sheets and an N-terminal α-helix^[3].

Function

Structure

Class B Structural Components

Helix I "Stalk" Region

Intracellular Helix VIII

Binding Pocket

Unique components to the GPCR

The 7tm region has a conserved disulfide bond at which helps to stabilize the 7tm fold. This bond is conserved among both Class A and Class B receptors.

The ECD region of Class B GCPRs is defined by three conserved disulfide bonds. These bonds occur at , , and .

Glucagon Binding

conformational states

Clinical Relevance

Because of this, it is being looked as a potential drug target for Type 2 diabetes.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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
↑ Yang L, Yang D, de Graaf C, Moeller A, West GM, Dharmarajan V, Wang C, Siu FY, Song G, Reedtz-Runge S, Pascal BD, Wu B, Potter CS, Zhou H, Griffin PR, Carragher B, Yang H, Wang MW, Stevens RC, Jiang H. Conformational states of the full-length glucagon receptor. Nat Commun. 2015 Jul 31;6:7859. doi: 10.1038/ncomms8859. PMID:26227798 doi:http://dx.doi.org/10.1038/ncomms8859

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1167"

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 == Background ==
-The human glucagon receptor is one of 15 secretin-like, or Class B, members of G-protein-coupled receptors (GCPRs). Like other GCPRs, it has a 7 trans-membrane helical domain (<scene name='72/721538/7tm_labeled_helicies/3'>Labeled Helices of 7tm </scene>) and a globular N-terminus extracellular domain (<scene name='72/721538/Ecd/2'>ECD</scene>).
+The human glucagon receptor is one of 15 secretin-like, or Class B, members of G-protein-coupled receptors (GCPRs). Like other GCPRs, it has a <scene name='72/721538/7tm_labeled_helicies/3'>7 trans-membrane </scene> helical domain (shown in blue) and a globular N-terminus extracellular domain (<scene name='72/721538/Ecd/2'>ECD</scene>). As its name suggests, the 7tm is made up of alpha helices that pass through the membrane seven times.
 During times of fasting (or low blood sugar) the pancreas dispatches glucagon to activate the GCPR in the liver, which causes the release of glucose into the blood.