1LL8

Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation

1LL8 の概要

• エントリーDOI: 10.2210/pdb1ll8/pdb
• NMR情報: BMRB: 5354
• 分子名称: PAS Kinase (1 entity in total)
• 機能のキーワード: pas domain, ligand binding, ligand screening, kinase regulation, transferase
• 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: 12659.52

構造登録者

Amezcua, C.A.,Harper, S.M.,Rutter, J.,Gardner, K.H. (登録日: 2002-04-26, 公開日: 2002-10-09, 最終更新日: 2024-05-01)

主引用文献

Amezcua, C.A.,Harper, S.M.,Rutter, J.,Gardner, K.H.
Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.
Structure, 10:1349-1361, 2002

PubMed Abstract: PAS domains are sensory modules in signal-transducing proteins that control responses to various environmental stimuli. To examine how those domains can regulate a eukaryotic kinase, we have studied the structure and binding interactions of the N-terminal PAS domain of human PAS kinase using solution NMR methods. While this domain adopts a characteristic PAS fold, two regions are unusually flexible in solution. One of these serves as a portal that allows small organic compounds to enter into the core of the domain, while the other binds and inhibits the kinase domain within the same protein. Structural and functional analyses of point mutants demonstrate that the compound and ligand binding regions are linked, suggesting that the PAS domain serves as a ligand-regulated switch for this eukaryotic signaling system.

PubMed: 12377121
DOI: 10.1016/S0969-2126(02)00857-2

実験手法

SOLUTION NMR