Sandbox Reserved 1167: Difference between revisions

[[Image:7tm_labeled_with_membrane.png|200 px|left|thumb|The 7tm spans the cell membrane]]The human glucagon receptor (GCGR) is one of 15 secretin-like, or Class B, G-protein-coupled receptors (GPCRs). Like other GPCRs, 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. The extracellular domain has an α-β-β structure that consists of two antiparallel β-sheets and a N-terminal α-helix<ref>PMID:26227798</ref>.  

Because of GCGR's role in glucose homeostasis, it is a potential drug target for Type 2 diabetes. Specifically, molecules that antagoinze the glucagon receptor may be able to lower blood sugar levels. Studies have shown that two antibodies, mAb1 and mAb23, target the ECD domain of the GCGR interrupt glucagon binding<ref>PMID:22908259</ref>. Disrupting the normal interactions between the ECD and the 7tm domains, these antibiotics inhibit the receptor's function and help to lower blood glucose level. Additional research has shown that another antibody, mAb7, inhibits GCGR allosterically<ref>PMID:24189067</ref>. Binding to a site outside of the binding pocket, mAb7 inhibits the receptor without interacting with essential glucagon binding residues.