1IA8

THE 1.7 A CRYSTAL STRUCTURE OF HUMAN CELL CYCLE CHECKPOINT KINASE CHK1

1IA8 の概要

• エントリーDOI: 10.2210/pdb1ia8/pdb
• 分子名称: CHK1 CHECKPOINT KINASE, SULFATE ION (3 entities in total)
• 機能のキーワード: protein kinase, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: O14757
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33139.05

構造登録者

Chen, P.,Luo, C.,Deng, Y.,Ryan, K.,Register, J.,Margosiak, S.,Tempczyk-Russell, A.,Nguyen, B.,Myers, P.,Lundgren, K.,Chen Kan, C.-C.,O'Connor, P.M. (登録日: 2001-03-22, 公開日: 2001-04-18, 最終更新日: 2024-04-03)

主引用文献

Chen, P.,Luo, C.,Deng, Y.,Ryan, K.,Register, J.,Margosiak, S.,Tempczyk-Russell, A.,Nguyen, B.,Myers, P.,Lundgren, K.,Kan, C.C.,O'Connor, P.M.
The 1.7 A crystal structure of human cell cycle checkpoint kinase Chk1: implications for Chk1 regulation.
Cell(Cambridge,Mass.), 100:681-692, 2000

PubMed Abstract: The checkpoint kinase Chk1 is an important mediator of cell cycle arrest following DNA damage. The 1.7 A resolution crystal structures of the human Chk1 kinase domain and its binary complex with an ATP analog has revealed an identical open kinase conformation. The secondary structure and side chain interactions stabilize the activation loop of Chk1 and enable kinase activity without phosphorylation of the catalytic domain. Molecular modeling of the interaction of a Cdc25C peptide with Chk1 has uncovered several conserved residues that are important for substrate selectivity. In addition, we found that the less conserved C-terminal region negatively impacts Chk1 kinase activity.

PubMed: 10761933
DOI: 10.1016/S0092-8674(00)80704-7

実験手法

X-RAY DIFFRACTION (1.7 Å)