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Introduction

, also known as secretin-like receptors, are a subfamily of the more well known class A (rhodopsin-like) glucagon receptor family. Located in the liver, class B glucagon receptors (GCGRs) are activated by the binding of the hormonal peptide glucagon which leads to the release of glucose into the bloodstream and plays an essential role in 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

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

Structural highlights

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