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Background
The human glucagon receptor is one of 15 secretin-like, or Class B, members of G-protein-coupled receptors (GCPRs).
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. Because of this, it is being looked as a potential drug target for Type 2 diabetes.
Secretin-like GPCRs contains both a 7tm domain (blue) and a globular N-terminus ECD (magenta)
The Extracellular Domain () has a α-β-β structure which consists of two antiparallel β-sheets and an N-terminal α-helix[3].
Function
Structure
Class B Structural Components
Helix I "Stalk" Region
Intracellular Helix VIII
Binding Pocket
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 .
Clinical Relevance
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