Sandbox Reserved 1166

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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class B Human Glucagon Receptorclass B Human Glucagon Receptor

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BackgroundBackground

G-protein coupled receptors

StructureStructure

transmembrane protein

alpha helix

Class B structural componentsClass 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 bond

As a part of the interface 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 GPCRunique 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 RelevanceClinical Relevance

clinical relevance