Sandbox Reserved 1167: Difference between revisions

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== Background ==
== Background ==
[[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>.  
[[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, [https://en.wikipedia.org/wiki/G_protein%E2%80%93coupled_receptor 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>.