1F3M

CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1

Summary for 1F3M

• Entry DOI: 10.2210/pdb1f3m/pdb
• Descriptor: SERINE/THREONINE-PROTEIN KINASE PAK-ALPHA, IODIDE ION, ... (4 entities in total)
• Functional Keywords: kinase domain, autoinhibitory fragment, homodimer, transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q13153 Q13153
• Total number of polymer chains: 4
• Total formula weight: 88460.21

Authors

Lei, M.,Lu, W.,Meng, W.,Parrini, M.-C.,Eck, M.J.,Mayer, B.J.,Harrison, S.C. (deposition date: 2000-06-05, release date: 2000-06-29, Last modification date: 2024-02-07)

Primary citation

Lei, M.,Lu, W.,Meng, W.,Parrini, M.C.,Eck, M.J.,Mayer, B.J.,Harrison, S.C.
Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch.
Cell(Cambridge,Mass.), 102:387-397, 2000

PubMed 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).

PubMed: 10975528
DOI: 10.1016/S0092-8674(00)00043-X

Experimental method

X-RAY DIFFRACTION (2.3 Å)