1UA2

Crystal Structure of Human CDK7

1UA2 の概要

• エントリーDOI: 10.2210/pdb1ua2/pdb
• 分子名称: Cell division protein kinase 7, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: cell cycle; phosphorylation; protein-protein interaction; protein kinase, cell cycle, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P50613
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 158710.02

構造登録者

Lolli, G.,Lowe, E.D.,Brown, N.R.,Johnson, L.N. (登録日: 2004-08-11, 公開日: 2004-12-07, 最終更新日: 2024-11-20)

主引用文献

Lolli, G.,Lowe, E.D.,Brown, N.R.,Johnson, L.N.
The Crystal Structure of Human CDK7 and Its Protein Recognition Properties
Structure, 12:2067-2079, 2004

PubMed Abstract: CDK7, a member of the cyclin-dependent protein kinase family, regulates the activities of other CDKs through phosphorylation on their activation segment and hence contributes to control of the eukaryotic cell cycle. CDK7 also assists in the regulation of transcription as part of the transcription factor TFIIH complex. For maximum activity and stability, CDK7 requires phosphorylation, association with cyclin H, and association with a third protein, MAT1. We have determined the crystal structure of human CDK7 in complex with ATP at 3 A resolution. The kinase is in the inactive conformation, similar to that observed for inactive CDK2. The activation segment is phosphorylated at Thr170 and is in a defined conformation that differs from that in phospho-CDK2 and phospho-CDK2/cyclin A. The functional properties of the enzyme against CDK2 and CTD as substrates are characterized through kinase assays. Experiments confirm that CDK7 is not a substrate for kinase-associated phosphatase.

PubMed: 15530371
DOI: 10.1016/j.str.2004.08.013

実験手法

X-RAY DIFFRACTION (3.02 Å)