2v6v
From Proteopedia
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Revision as of 15:38, 30 October 2007
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THE STRUCTURE OF THE BEM1P PX DOMAIN
Overview
Phox homology (PX) domains, which have been identified in a variety of, proteins involved in cell signaling and membrane trafficking, have been, shown to interact with phosphoinositides (PIs) with different affinities, and specificities. To elucidate the structural origin of diverse PI, specificity of PX domains, we determined the crystal structure of the PX, domain from Bem1p, which has been reported to bind, phosphatidylinositol-4-phosphate (PtdIns4P). We also measured the membrane, binding properties of the PX domain and its mutants by surface plasmon, resonance and monolayer techniques and calculated the electrostatic, potentials for the PX domain in the absence and presence of bound, PtdIns4P. The Bem1p PX domain contains a signature PI-binding site, optimized for PtdIns4P binding ... [(full description)]
About this Structure
2V6V is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with DTT as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural and membrane binding analysis of the PX domain of Bem1p: Basis of phosphatidylinositol-4-phosphate specificity., Stahelin RV, Karathanassis D, Murray D, Williams RL, Cho W, J Biol Chem. 2007 Jun 20;. PMID:17581820
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