Sandbox28: Difference between revisions
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There are also two active sites that can be seen here: <scene name='Sandbox28/Ac1/1'>active site 1</scene> <scene name='Sandbox28/Ac2/1'>active site 2</scene> | There are also two active sites that can be seen here: <scene name='Sandbox28/Ac1/1'>active site 1</scene> <scene name='Sandbox28/Ac2/1'>active site 2</scene> | ||
Publication Abstract from PubMed | |||
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. | |||
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 | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. | |||
{{STRUCTURE_1h8f | PDB=1h8f | SCENE= }} | |||
