3q52 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
p21-activated kinases (PAKs) play an important role in diverse cellular processes. Full activation of PAKs requires autophosphorylation of a critical threonine/serine located in the activation loop of the kinase domain. Here we report crystal structures of the phosphorylated and unphosphorylated PAK1 kinase domain. The phosphorylated PAK1 kinase domain has a conformation typical of all active protein kinases. Interestingly, the structure of the unphosphorylated PAK1 kinase domain reveals an unusual dimeric arrangement expected in an authentic enzyme-substrate complex, in which the activation loop of the putative "substrate" is projected into the active site of the "enzyme." The enzyme is bound to AMP-PNP and has an active conformation, whereas the substrate is empty and adopts an inactive conformation. Thus, the structure of the asymmetric homodimer mimics a trans-autophosphorylation complex, and suggests that unphosphorylated PAK1 could dynamically adopt both the active and inactive conformations in solution.
Structural insights into the autoactivation mechanism of p21-activated protein kinase.,Wang J, Wu JW, Wang ZX Structure. 2011 Dec 7;19(12):1752-61. PMID:22153498[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Wang J, Wu JW, Wang ZX. Structural insights into the autoactivation mechanism of p21-activated protein kinase. Structure. 2011 Dec 7;19(12):1752-61. PMID:22153498 doi:10.1016/j.str.2011.10.013
