2c30

File:2c30.gif

spinqualitylabelsall models 2c30, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE HUMAN P21-ACTIVATED KINASE 6

OverviewOverview

p21-activated kinases have been classified into two groups based on their, domain architecture. Group II PAKs (PAK4-6) regulate a wide variety of, cellular functions, and PAK deregulation has been linked to tumor, development. Structural comparison of five high-resolution structures, comprising all active, monophosphorylated group II catalytic domains, revealed a surprising degree of domain plasticity, including a number of, catalytically productive and nonproductive conformers. Rearrangements of, helix alphaC, a key regulatory element of kinase function, resulted in an, additional helical turn at the alphaC N terminus and a distortion of its C, terminus, a movement hitherto unseen in protein kinases. The observed, structural changes led to the formation of interactions between conserved, residues that structurally link the glycine-rich loop, alphaC, and the, activation segment and firmly anchor alphaC in an active conformation., Inhibitor screening identified six potent PAK inhibitors from which a, tri-substituted purine inhibitor was cocrystallized with PAK4 and PAK5.

About this StructureAbout this Structure

2C30 is a Single protein structure of sequence from Homo sapiens with PO4 and CL 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.

ReferenceReference

Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs., Eswaran J, Lee WH, Debreczeni JE, Filippakopoulos P, Turnbull A, Fedorov O, Deacon SW, Peterson JR, Knapp S, Structure. 2007 Feb;15(2):201-13. PMID:17292838

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