1f3m

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spinqualitylabelsall models 1f3m, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1

Overview

The p21-activated kinases (PAKs), stimulated by binding with GTP-liganded, forms of Cdc42 or Rac, modulate cytoskeletal actin assembly and activate, MAP-kinase pathways. The 2.3 A resolution crystal structure of a complex, between the N-terminal autoregulatory fragment and the C-terminal kinase, domain of PAK1 shows that GTPase binding will trigger a series of, conformational changes, beginning with disruption of a PAK1 dimer and, ending with rearrangement of the kinase active site into a catalytically, competent state. An inhibitory switch (IS) domain, which overlaps the, GTPase binding region of PAK1, positions a polypeptide segment across the, kinase cleft. GTPase binding will refold part of the IS domain and unfold, the rest. A related switch has been seen in the Wiskott-Aldrich syndrome, protein (WASP).

About this Structure

1F3M is a Single protein structure of sequence from Homo sapiens with IOD as ligand. Full crystallographic information is available from OCA.

Reference

Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch., Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC, Cell. 2000 Aug 4;102(3):387-97. PMID:10975528

Page seeded by OCA on Mon Nov 12 16:48:45 2007