We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Sandbox Reserved 1165
From Proteopedia
(Difference between revisions)
| Line 5: | Line 5: | ||
==Introduction== | ==Introduction== | ||
| - | <scene name='72/721536/Class_b_receptor/1'>Human glucagon class B G protein-coupled receptors (GPCRs)</scene>, also known as secretin-like receptors, are a subfamily of the more well known class A ([https://en.wikipedia.org/wiki/Rhodopsin-like_receptors rhodopsin-like]) glucagon receptor family. Located in the liver, class B glucagon receptors (GCGRs) are activated by the binding of the hormonal peptide [https://en.wikipedia.org/wiki/Glucagon glucagon] which leads to the release of glucose into the bloodstream and plays an essential role in [https://en.wikipedia.org/wiki/Glucose glucose] homeostasis. Class B GCGRs are composed of a seven transmembrane domain (7TM) and extracellular domain ( | + | <scene name='72/721536/Class_b_receptor/1'>Human glucagon class B G protein-coupled receptors (GPCRs)</scene>, also known as secretin-like receptors, are a subfamily of the more well known class A ([https://en.wikipedia.org/wiki/Rhodopsin-like_receptors rhodopsin-like]) glucagon receptor family. Located in the liver, class B glucagon receptors (GCGRs) are activated by the binding of the hormonal peptide [https://en.wikipedia.org/wiki/Glucagon glucagon] which leads to the release of glucose into the bloodstream and plays an essential role in [https://en.wikipedia.org/wiki/Glucose glucose] homeostasis. Class B GCGRs are composed of a seven transmembrane domain (7TM) and extracellular domain (ECD) that are of vital importance in glucagon binding. In comparison, class A vs. class B glucagon receptors share less than fifteen percent sequence homology, but both share this 7TM which is a primary area of comparison between the two. |
== Function == | == Function == | ||
[[Image:Proteopedia 2D.jpg |(|): |100 px|left|Figure Legend]] | [[Image:Proteopedia 2D.jpg |(|): |100 px|left|Figure Legend]] | ||
| - | == | + | == Structure == |
| + | Secretin-like receptors are composed entirely of alpha helices in their 7TM and ECD. A distinct feature of class B receptors is the N-terminal end of helix one in the 7TM. It extends an extra three helical turns into the ECD, and is longer than any of the class A receptors. This region, referred to as the "stalk" of class B receptors, is highly involved in glucagon binding and also helps in defining the orientation of the ECD with respect to the 7TM domain. | ||
| + | ==Extracellular Tips== | ||
| + | The locations of the extracellular tips for class B glucagon receptors allow for a much wider and deeper binding cavity in the ligand-binding pocket, which is much more immense than any of the class A GCGRs. | ||
| + | |||
| + | These wide ranges specifically occur between alpha helices two and six (green) and three and seven (red). | ||
== Relevance == | == Relevance == | ||
Revision as of 13:38, 15 March 2016
[[Image:]]
| 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:
More help: Help:Editing |
Human Glucagon Class B G Protein-Coupled Receptors (GPCRs)
| |||||||||||
