1f3m: Difference between revisions
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{{STRUCTURE_1f3m| PDB=1f3m | SCENE= }} | |||
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'''CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1''' | '''CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1''' | ||
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[[Category: Meng, W.]] | [[Category: Meng, W.]] | ||
[[Category: Parrini, M-C.]] | [[Category: Parrini, M-C.]] | ||
[[Category: | [[Category: Autoinhibitory fragment]] | ||
[[Category: | [[Category: Homodimer]] | ||
[[Category: | [[Category: Kinase domain]] | ||
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Revision as of 12:51, 2 May 2008
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. 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 Fri May 2 15:51:13 2008
