Sandbox Reserved 1167

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Revision as of 13:22, 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.

To get started:

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.

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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, G-protein-coupled receptors (GCPRs). Like other GCPRs, it has a helical domain (shown in blue) and a globular N-terminus (shown in magenta). As its name suggests, the 7tm is made up of alpha helices that pass through the membrane seven times.

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

Function

The Glucagon Receptor plays an important role in glucose homeostasis. 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.

Structure

Class B Structural Components

Helix I "Stalk" Region

The of Helix I is longer than any other class of GCPR and extends 3 α-helical turns above the plane of the membrane. It helps to capture the glucagon peptide and facilitates it's insertion into the 7tm.

Intracellular Helix VIII

Binding Pocket

The Class B GCPR as the longest and deepest binding pocket. The distance between the EC tips of Helicies II and VI are the largest among the GCPRs and the distance

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. Molecules that antagoinze the glucagon receptor may be able to lower blood sugar levels.

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"

@@ Line 9: / Line 9: @@
 The human glucagon receptor is one of 15 secretin-like, or Class B, 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 <scene name='72/721538/Ecd/2'>extracellular domain</scene> (shown in magenta). 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)
@@ Line 20: / Line 17: @@
 == Function ==
+The Glucagon Receptor plays an important role in glucose homeostasis. 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.
 == Structure ==
@@ Line 26: / Line 26: @@
 ==== Helix I "Stalk" Region ====
+The <scene name='72/721538/Helix_i/14'>"Stalk" Region</scene> of Helix I is longer than any other class of GCPR and extends 3 α-helical turns above the plane of the membrane. It helps to capture the glucagon peptide and facilitates it's insertion into the 7tm.
-<scene name='72/721538/Helix_i/15'>Helix I</scene>
-<scene name='72/721538/Helix_i/14'>"Stalk" Region</scene>
 ==== Intracellular Helix VIII ====
 ==== Binding Pocket ====
+The Class B GCPR as the longest and deepest binding pocket. The distance between the EC tips of Helicies II and VI are the largest among the GCPRs and the distance
 === Unique components to the GPCR ===
@@ Line 46: / Line 46: @@
 == Clinical Relevance ==
-Because of this, it is being looked as a potential drug target for Type 2 diabetes.
+Because of this, it is being looked as a potential drug target for Type 2 diabetes. Molecules that antagoinze the glucagon receptor may be able to lower blood sugar levels.
 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.