1kcm: Difference between revisions

Revision as of 10:08, 2 July 2008

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File:1kcm.png

Template:STRUCTURE 1kcm

Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms ResolutionCrystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution

Template:ABSTRACT PUBMED 11980708

About this StructureAbout this Structure

1KCM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association., Schouten A, Agianian B, Westerman J, Kroon J, Wirtz KW, Gros P, EMBO J. 2002 May 1;21(9):2117-21. PMID:11980708

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OCA

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-'''Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution'''
+===Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution===
-==Overview==
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-Phosphatidylinositol transfer protein alpha (PITP alpha) is a ubiquitous and highly conserved protein in multicellular eukaryotes that catalyzes the exchange of phospholipids between membranes in vitro and participates in cellular phospholipid metabolism, signal transduction and vesicular trafficking in vivo. Here we report the three-dimensional crystal structure of a phospholipid-free mouse PITP alpha at 2.0 A resolution. The structure reveals an open conformation characterized by a channel running through the protein. The channel is created by opening the phospholipid-binding cavity on one side by displacement of the C-terminal region and a hydrophobic lipid exchange loop, and on the other side by flattening of the central beta-sheet. The relaxed conformation is stabilized at the proposed membrane association site by hydrophobic interactions with a crystallographically related molecule, creating an intimate dimer. The observed open conformer is consistent with a membrane-bound state of PITP and suggests a mechanism for membrane anchoring and the presentation of phosphatidylinositol to kinases and phospholipases after its extraction from the membrane. Coordinates have been deposited in the Protein Data Bank (accession No. 1KCM).
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 [[Category: Phospholipid transport]]
 [[Category: Pitp]]
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