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    Cell. 2000 Aug 4;102(3):387-97.

    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.

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    Laboratory of Molecular Medicine, Children's Hospital, Boston, Massachusetts 02115, USA.

    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).

    PMID:
    10975528
    [PubMed - indexed for MEDLINE]

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