1ll8
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(New page: 200px<br /> <applet load="1ll8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ll8" /> '''Structure and interactions of PAS kinase N-...)
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Revision as of 15:55, 12 November 2007
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Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
Overview
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.
About this Structure
1LL8 is a Single protein structure of sequence from Homo sapiens. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation., Amezcua CA, Harper SM, Rutter J, Gardner KH, Structure. 2002 Oct;10(10):1349-61. PMID:12377121
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