1B39

HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160

1B39 の概要

• エントリーDOI: 10.2210/pdb1b39/pdb
• 分子名称: PROTEIN (CELL DIVISION PROTEIN KINASE 2), MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: protein kinase, transferase, serine/threonine protein kinase, atp-binding, cell cycle, cell division, mitosis, phosphorylation
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34534.01

構造登録者

Brown, N.R.,Noble, M.E.M.,Lawrie, A.M.,Morris, M.C.,Tunnah, P.,Divita, G.,Johnson, L.N.,Endicott, J.A. (登録日: 1998-12-17, 公開日: 1998-12-23, 最終更新日: 2024-11-06)

主引用文献

Brown, N.R.,Noble, M.E.,Lawrie, A.M.,Morris, M.C.,Tunnah, P.,Divita, G.,Johnson, L.N.,Endicott, J.A.
Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity.
J.Biol.Chem., 274:8746-8756, 1999

PubMed Abstract: We have prepared phosphorylated cyclin-dependent protein kinase 2 (CDK2) for crystallization using the CDK-activating kinase 1 (CAK1) from Saccharomyces cerevisiae and have grown crystals using microseeding techniques. Phosphorylation of monomeric human CDK2 by CAK1 is more efficient than phosphorylation of the binary CDK2-cyclin A complex. Phosphorylated CDK2 exhibits histone H1 kinase activity corresponding to approximately 0.3% of that observed with the fully activated phosphorylated CDK2-cyclin A complex. Fluorescence measurements have shown that Thr160 phosphorylation increases the affinity of CDK2 for both histone substrate and ATP and decreases its affinity for ADP. By contrast, phosphorylation of CDK2 has a negligible effect on the affinity for cyclin A. The crystal structures of the ATP-bound forms of phosphorylated CDK2 and unphosphorylated CDK2 have been solved at 2.1-A resolution. The structures are similar, with the major difference occurring in the activation segment, which is disordered in phosphorylated CDK2. The greater mobility of the activation segment in phosphorylated CDK2 and the absence of spontaneous crystallization suggest that phosphorylated CDK2 may adopt several different mobile states. The majority of these states are likely to correspond to inactive conformations, but a small fraction of phosphorylated CDK2 may be in an active conformation and hence explain the basal activity observed.

PubMed: 10085115
DOI: 10.1074/jbc.274.13.8746

実験手法

X-RAY DIFFRACTION (2.1 Å)