3w67: Difference between revisions
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==Crystal structure of mouse alpha-tocopherol transfer protein in complex with alpha-tocopherol and phosphatidylinositol-(3,4)-bisphosphate== | |||
<StructureSection load='3w67' size='340' side='right' caption='[[3w67]], [[Resolution|resolution]] 2.61Å' scene=''> | |||
{{ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3w67]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W67 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PT:(2R)-3-{[(S)-HYDROXY{[(1S,2R,3R,4S,5S,6S)-2,3,6-TRIHYDROXY-4,5-BIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL]OXY}PROPANE-1,2-DIYL+DIBUTANOATE'>3PT</scene>, <scene name='pdbligand=VIV:(2R)-2,5,7,8-TETRAMETHYL-2-[(4R,8R)-4,8,12-TRIMETHYLTRIDECYL]CHROMAN-6-OL'>VIV</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ttpa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w67 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w67 RCSB], [http://www.ebi.ac.uk/pdbsum/3w67 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
alpha-Tocopherol (vitamin E) transfer protein (alpha-TTP) regulates the secretion of alpha-tocopherol from liver cells. Missense mutations of some arginine residues at the surface of alpha-TTP cause severe vitamin E deficiency in humans, but the role of these residues is unclear. Here, we found that wild-type alpha-TTP bound phosphatidylinositol phosphates (PIPs), whereas the arginine mutants did not. In addition, PIPs in the target membrane promoted the intermembrane transfer of alpha-tocopherol by alpha-TTP. The crystal structure of the alpha-TTP-PIPs complex revealed that the disease-related arginine residues interacted with phosphate groups of the PIPs and that the PIPs binding caused the lid of the alpha-tocopherol-binding pocket to open. Thus, PIPs have a role in promoting the release of a ligand from a lipid-transfer protein. | |||
Impaired alpha-TTP-PIPs Interaction Underlies Familial Vitamin E Deficiency.,Kono N, Ohto U, Hiramatsu T, Urabe M, Uchida Y, Satow Y, Arai H Science. 2013 Apr 18. PMID:23599266<ref>PMID:23599266</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Ohto, U | [[Category: Ohto, U]] | ||
[[Category: Satow, Y | [[Category: Satow, Y]] | ||
[[Category: Alpha-tocopherol]] | [[Category: Alpha-tocopherol]] | ||
[[Category: Alpha-tocopherol transfer]] | [[Category: Alpha-tocopherol transfer]] | ||
Revision as of 07:03, 21 December 2014
Crystal structure of mouse alpha-tocopherol transfer protein in complex with alpha-tocopherol and phosphatidylinositol-(3,4)-bisphosphate
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