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Sandbox Reserved 1166

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Revision as of 13:10, 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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Click the edit this page tab at the top. Save the page after each step, then edit it again.
Click the 3D button (when editing, above the wikitext box) to insert Jmol.
show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

class B Human Glucagon Receptor

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 GPCR
4 Clinical Relevance
5 References

Background

G-protein coupled receptors

Function

Structure

Class B structural components

As opposed to class A glucagon receptors which have a proline kink, in all secretin-like class B glucagon receptors there is a Glycine at position 393 in Helix VII which allows for a . This Glycine and therefore this helical bend is fully conserved in all secretin-like class B receptors and is an important part of the FQGxxVxxYCF motif.

Another important structural component found in all secretin-like class B receptors are the two conserved salt bridges found between Arg 346 and Glu 406 and Arg 173 and Glu 406

Glu 406 Salt Bridges

Since there is no conservation of these residues in class A receptors these salt bridges are likely an important feature of secretin-like class B receptors.

Disulfide bonds

As a part of the interface stabilization between helices VI, V, and III, a class B specific hydrogen bond occurs between N 318 of Helix V and L 242 of Helix III.

unique components to GPCR

An important interface stabilization interaction between helices I and VII occurs between Ser 152 of Helix I and Ser 390 of Helix VII. Due to their close proximity to one another, they form an important which serves to stabilize the structure of GCGR.

Clinical Relevance

clinical relevance

</StructureSection>

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

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1166"

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 == Background ==
-[https://en.wikipedia.org/wiki/Glucagon_receptor]
+[https://en.wikipedia.org/wiki/G_protein%E2%80%93coupled_receptor G-protein coupled receptors]
 == Function ==
@@ Line 26: / Line 27: @@
 == Clinical Relevance ==
+[https://en.wikipedia.org/wiki/Glucagon_receptor clinical relevance]
-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.
 </StructureSection>
 == References ==
 <references/>

Sandbox Reserved 1166

From Proteopedia

Revision as of 13:10, 29 March 2016

class B Human Glucagon Receptor

Contents

Background

Function

Structure

Class B structural components

unique components to GPCR

Clinical Relevance

References

Views

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