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1t27
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(New page: 200px<br /><applet load="1t27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t27, resolution 2.20Å" /> '''THE STRUCTURE OF PIT...)
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Revision as of 00:48, 21 November 2007
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THE STRUCTURE OF PITP COMPLEXED TO PHOSPHATIDYLCHOLINE
Overview
Eukaryotic phosphatidylinositol transfer protein is a ubiquitous, multifunctional protein that transports phospholipids between membrane, surfaces and participates in cellular phospholipid metabolism during, signal transduction and vesicular trafficking. The three-dimensional, structure of the alpha-isoform of rat phosphatidylinositol transfer, protein complexed with one molecule of phosphatidylcholine, one of its, physiological ligands, has been determined to 2.2 A resolution by x-ray, diffraction techniques. A single beta-sheet and several long alpha-helices, define an enclosed internal cavity in which a single molecule of the, phospholipid is accommodated with its polar head group in the center of, the protein and fatty acyl chains projected toward the surface. Other, structural features suggest mechanisms by which cytosolic, phosphatidylinositol transfer protein interacts with membranes for lipid, exchange and associates with a variety of lipid and protein kinases.
About this Structure
1T27 is a Single protein structure of sequence from Rattus norvegicus with PCW as ligand. This structure superseeds the now removed PDB entry 1FVZ. Full crystallographic information is available from OCA.
Reference
Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine., Yoder MD, Thomas LM, Tremblay JM, Oliver RL, Yarbrough LR, Helmkamp GM Jr, J Biol Chem. 2001 Mar 23;276(12):9246-52. Epub 2000 Dec 4. PMID:11104777
Page seeded by OCA on Wed Nov 21 02:56:04 2007
