Reference: Lei M, et al. (2000)
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Abstract
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).
- Reference Type
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Journal Article |
Research Support, Non-U.S. Gov't |
Research Support, U.S. Gov't, P.H.S.
- Authors
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Lei M,
Lu W,
Meng W,
Parrini MC,
Eck MJ,
Mayer BJ,
Harrison SC
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