Journal
CELL
Volume 102, Issue 3, Pages 387-397Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(00)00043-X
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Funding
- NCI NIH HHS [1R01 CA2258-01] Funding Source: Medline
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The p21-activated kinases (PAKs), stimulated by binding with GTP-liganded forms of Cdc42 or Pac, modulate cytoskeletal actin assembly and activate MAP-kinase pathways. The 2.3 Angstrom 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).
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