1JKL

1.6A X-RAY STRUCTURE OF BINARY COMPLEX OF A CATALYTIC DOMAIN OF DEATH-ASSOCIATED PROTEIN KINASE WITH ATP ANALOGUE

1JKL の概要

• エントリーDOI: 10.2210/pdb1jkl/pdb
• 分子名称: DEATH-ASSOCIATED PROTEIN KINASE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P53355
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34300.56

構造登録者

Tereshko, V.,Teplova, M.,Brunzelle, J.,Watterson, D.M.,Egli, M. (登録日: 2001-07-12, 公開日: 2002-04-01, 最終更新日: 2024-02-07)

主引用文献

Tereshko, V.,Teplova, M.,Brunzelle, J.,Watterson, D.M.,Egli, M.
Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression.
Nat.Struct.Biol., 8:899-907, 2001

PubMed Abstract: 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.

PubMed: 11573098
DOI: 10.1038/nsb1001-899

実験手法

X-RAY DIFFRACTION (1.62 Å)