1o6l
From Proteopedia
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CRYSTAL STRUCTURE OF AN ACTIVATED AKT/PROTEIN KINASE B (PKB-PIF CHIMERA) TERNARY COMPLEX WITH AMP-PNP AND GSK3 PEPTIDE
Overview
The protein kinase Akt/PKB is stimulated by the phosphorylation of two, regulatory residues, Thr 309 of the activation segment and Ser 474 of the, hydrophobic motif (HM), that are structurally and functionally conserved, within the AGC kinase family. To understand the mechanism of PKB, regulation, we determined the crystal structures of activated kinase, domains of PKB in complex with a GSK3beta-peptide substrate and an ATP, analog. The activated state of the kinase was generated by phosphorylating, Thr 309 using PDK1 and mimicking Ser 474 phosphorylation either with the, S474D substitution or by replacing the HM of PKB with that of PIFtide, a, potent mimic of a phosphorylated HM. Comparison with the inactive PKB, structure indicates that the role of Ser 474 phosphorylation is to promote, ... [(full description)]
About this Structure
1O6L is a [Protein complex] structure of sequences from [Homo sapiens] with MN and ANP 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
Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP., Yang J, Cron P, Good VM, Thompson V, Hemmings BA, Barford D, Nat Struct Biol. 2002 Dec;9(12):940-4. PMID:12434148
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