1gng

From Proteopedia

Revision as of 13:10, 30 October 2007

GLYCOGEN SYNTHASE KINASE-3 BETA (GSK3) COMPLEX WITH FRATTIDE PEPTIDE

Overview

BACKGROUND: Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates, four serine residues on glycogen synthase (GS), in the sequence, SxxxSxxxSxxx-SxxxS(p), by recognizing and phosphorylating the first serine, in the sequence motif SxxxS(P) (where S(p) represents a phosphoserine)., FRATtide (a peptide derived from a GSK-3 binding protein) binds to GSK-3, and blocks GSK-3 from interacting with Axin. This inhibits the, Axin-dependent phosphorylation of beta-catenin by GSK-3. RESULTS:, Structures of uncomplexed Tyr216 phosphorylated GSK-3beta and of its, complex with a peptide and a sulfate ion both show the activation loop, adopting a conformation similar to that in the phosphorylated and active, forms of the related kinases CDK2 and ERK2. The sulfate ion, adjacent to, Val214 on the ... [(full description)]

About this Structure

1GNG is a [Protein complex] structure of sequences from [Homo sapiens] with SO4 and TRS as [ligands]. 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].

Reference

The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation., Bax B, Carter PS, Lewis C, Guy AR, Bridges A, Tanner R, Pettman G, Mannix C, Culbert AA, Brown MJ, Smith DG, Reith AD, Structure. 2001 Dec;9(12):1143-52. PMID:11738041

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