2iwl
From Proteopedia
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STRUCTURE OF THE PX DOMAIN OF PHOSPHOINOSITIDE 3-KINASE-C2ALPHA
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, specificities of PX domains, we determined the crystal structure of the PX, domain from phosphoinositide 3-kinase C2alpha (PI3K-C2alpha), which binds, phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)). To delineate the, mechanism by which this PX domain interacts with membranes, we measured, the membrane binding of the wild type domain and mutants by surface, plasmon resonance and monolayer techniques. This PX domain contains a, signature PI-binding site that is optimized for PtdIns(4,5)P(2) ... [(full description)]
About this Structure
2IWL is a [Single protein] structure of sequence from [Homo sapiens] with SO4 as [ligand]. Full crystallographic information is available from [OCA].
Reference
Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha., Stahelin RV, Karathanassis D, Bruzik KS, Waterfield MD, Bravo J, Williams RL, Cho W, J Biol Chem. 2006 Dec 22;281(51):39396-406. Epub 2006 Oct 12. PMID:17038310
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