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1f3m
From Proteopedia
CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1
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).
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1F3M is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell. 2000 Aug 4;102(3):387-97. PMID:10975528
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