1uw5

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1uw5, resolution 2.90Å

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STRUCTURE OF PITP-ALPHA COMPLEXED TO PHOSPHATIDYLINOSITOL

Overview

Phosphatidylinositol transfer protein alpha (PITPalpha) selectively, transports and promotes exchange of phosphatidylinositol (PI) and, phosphatidylcholine (PC) between lipid bilayers. In higher eukaryotes, PITPalpha is required for cellular functions such as phospholipase, C-mediated signaling, regulated exocytosis, and secretory vesicle, formation. We have determined the crystal structure of human PITPalpha, bound to its physiological ligand, PI, at 2.95 A resolution. The structure, identifies the critical side chains within the lipid-headgroup binding, pocket that define the exquisite specificity for PI. Mutational analysis, of the PI binding pocket is in good agreement with the structural data and, allows manipulation of functional properties of PITPalpha. Surprisingly, there are no ... [(full description)]

About this Structure

1UW5 is a [Single protein] structure of sequence from [Homo sapiens] with PIE as [ligand]. Full crystallographic information is available from [OCA].

Reference

Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol., Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ, Structure. 2004 Feb;12(2):317-26. PMID:14962392

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