1IA8

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

Summary for 1IA8

• Entry DOI: 10.2210/pdb1ia8/pdb
• Descriptor: CHK1 CHECKPOINT KINASE, SULFATE ION (3 entities in total)
• Functional Keywords: protein kinase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O14757
• Total number of polymer chains: 1
• Total formula weight: 33139.05

Authors

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. (deposition date: 2001-03-22, release date: 2001-04-18, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)