1f3m
From Proteopedia
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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 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 Thu Feb 21 12:34:31 2008
Categories: Homo sapiens | Single protein | Eck, M J. | Harrison, S C. | Lei, M. | Lu, W. | Mayer, B J. | Meng, W. | Parrini, M-C. | IOD | Autoinhibitory fragment | Homodimer | Kinase domain
