Structure and Interactions of PAS Kinase N-Terminal PAS Domain

阅读量：

作者：

CA Amezcua，SM Harper，J Rutter，KH Gardner

展开

摘要：

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.

展开

关键词：

PAS domain PAS kinase ligand binding kinase regulation NMR screening

DOI：

10.1016/S0969-2126(02)00857-2

被引量：

297

年份：

2002