Publication Abstract from PubMed
We have determined X-ray crystal structures with up to 1.5 A resolution of the catalytic domain of death-associated protein kinase (DAPK), the first described member of a novel family of pro-apoptotic and tumor-suppressive serine/threonine kinases. The geometry of the active site was studied in the apo form, in a complex with nonhydrolyzable AMPPnP and in a ternary complex consisting of kinase, AMPPnP and either Mg2+ or Mn2+. The structures revealed a previously undescribed water-mediated stabilization of the interaction between the lysine that is conserved in protein kinases and the beta- and gamma-phosphates of ATP, as well as conformational changes at the active site upon ion binding. Comparison between these structures and nucleotide triphosphate complexes of several other kinases disclosed a number of unique features of the DAPK catalytic domain, among which is a highly ordered basic loop in the N-terminal domain that may participate in enzyme regulation.
Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression.,Tereshko V, Teplova M, Brunzelle J, Watterson DM, Egli M Nat Struct Biol. 2001 Oct;8(10):899-907. PMID:11573098[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
