1h8f: Difference between revisions
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Revision as of 18:07, 12 November 2007
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GLYCOGEN SYNTHASE KINASE 3 BETA.
OverviewOverview
Glycogen synthase kinase 3 beta (GSK3 beta) plays a key role in insulin, and Wnt signaling, phosphorylating downstream targets by default, and, becoming inhibited following the extracellular signaling event. The, crystal structure of human GSK3 beta shows a catalytically active, conformation in the absence of activation-segment phosphorylation, with, the sulphonate of a buffer molecule bridging the activation-segment and, N-terminal domain in the same way as the phosphate group of the, activation-segment phospho-Ser/Thr in other kinases. The location of this, oxyanion binding site in the substrate binding cleft indicates direct, coupling of P+4 phosphate-primed substrate binding and catalytic, activation, explains the ability of GSK3 beta to processively, hyperphosphorylate substrates with Ser/Thr pentad-repeats, and suggests a, mechanism for autoinhibition in which the phosphorylated N terminus binds, as a competitive pseudosubstrate with phospho-Ser 9 occupying the P+4, site.
About this StructureAbout this Structure
1H8F is a Single protein structure of sequence from Homo sapiens with EPE as ligand. Active as Transferred entry: 2.7.11.1, with EC number 2.7.1.37 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition., Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH, Cell. 2001 Jun 15;105(6):721-32. PMID:11440715
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