Sandbox Reserved 433: Difference between revisions

The overall structure of GSK-3β has two phosphorylation sites that are involved in catalysis. One of these sites is Ser 9, resulting in the inactivation of GSK-3β. The second phosphorylation site is Tyr 216, located on the activation loop (<span style="color:green">'''green'''</span> ), and is responsible for the increase in catalytic activity. GSK-3β has the characteristic two-domain kinase fold, containing a N-terminal β-strand domain (<span style="color:Blue">'''light blue, residues 25-138'''</span>) and a C-terminal α-helical domain (<span style="color:red">'''red, residues 139-343'''</span>). There is an interface between the α and β domains, at which the ATP-binding site is located, encircled by the hinge and the glycine-rich loop.  The activation loop (<span style="color:purple">'''purple'''</span>) runs along the surface of the substrate-binding groove. There are 39 residues in the C-terminus end that are outside the main kinase fold.  These residues form a small domain that closely packs next to the α-helical domain.  The β-strand domain is formed by seven β-strands that run in an antiparallel formation. Strands 2-6 form a β-barrel, through which a short α helix (<span style="color:orange">'''yellow, residues 96-102'''</span>) aligns against the β-barrel <ref name="overall">PMID: 11427888</ref>.