2JFL

CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE (DIPHOSPHORYLATED FORM) BOUND TO 5- AMINO-3-((4-(AMINOSULFONYL)PHENYL)AMINO)-N-(2,6- DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE

2JFL の概要

• エントリーDOI: 10.2210/pdb2jfl/pdb
• 関連するPDBエントリー: 2J51 2JA0 2JFM
• 分子名称: STE20-LIKE SERINE/THREONINE-PROTEIN KINASE, 5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: transferase, serine/threonine-protein kinase, atp-binding, phosphorylation, muscle development, kinase, apoptosis, germinal centre kinase, serine- threonine kinase 2, nucleotide-binding, serine-threonine-protein kinase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm : Q9H2G2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38151.34

構造登録者

Pike, A.C.W.,Rellos, P.,Fedorov, O.,Keates, T.,Salah, E.,Savitsky, P.,Papagrigoriou, E.,Bunkoczi, G.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.,Weigelt, J.,Sundstrom, M.,Knapp, S. (登録日: 2007-02-02, 公開日: 2007-02-27, 最終更新日: 2024-11-20)

主引用文献

Pike, A.C.W.,Rellos, P.,Niesen, F.H.,Turnbull, A.,Oliver, A.W.,Parker, S.A.,Turk, B.E.,Pearl, L.H.,Knapp, S.
Activation Segment Dimerization: A Mechanism for Kinase Autophosphorylation of Non-Consensus Sites.
Embo J., 27:704-, 2008

PubMed Abstract: Protein kinase autophosphorylation of activation segment residues is a common regulatory mechanism in phosphorylation-dependent signalling cascades. However, the molecular mechanisms that guarantee specific and efficient phosphorylation of these sites have not been elucidated. Here, we report on three novel and diverse protein kinase structures that reveal an exchanged activation segment conformation. This dimeric arrangement results in an active kinase conformation in trans, with activation segment phosphorylation sites in close proximity to the active site of the interacting protomer. Analytical ultracentrifugation and chemical cross-linking confirmed the presence of dimers in solution. Consensus substrate sequences for each kinase showed that the identified activation segment autophosphorylation sites are non-consensus substrate sites. Based on the presented structural and functional data, a model for specific activation segment phosphorylation at non-consensus substrate sites is proposed that is likely to be common to other kinases from diverse subfamilies.

PubMed: 18239682
DOI: 10.1038/EMBOJ.2008.8

実験手法

X-RAY DIFFRACTION (2.2 Å)