View source for 3w68


==Crystal structure of mouse alpha-tocopherol transfer protein in complex with alpha-tocopherol and phosphatidylinositol-(4,5)-bisphosphate==
<StructureSection load='3w68' size='340' side='right'caption='[[3w68]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3w68]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W68 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4PT:(2R)-3-{[(S)-{[(2S,3R,5S,6S)-2,6-DIHYDROXY-3,4,5-TRIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-(1-HYDROXYBUTOXY)PROPYL+BUTYRATE'>4PT</scene>, <scene name='pdbligand=PBU:(2R)-3-{[(R)-HYDROXY{[(1R,2R,3S,4R,5R,6S)-2,3,6-TRIHYDROXY-4,5-BIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL]OXY}PROPANE-1,2-DIYL+DIBUTANOATE'>PBU</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3w68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w68 OCA], [https://pdbe.org/3w68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w68 RCSB], [https://www.ebi.ac.uk/pdbsum/3w68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w68 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TTPA_MOUSE TTPA_MOUSE] Binds alpha-tocopherol and enhances its transfer between separate membranes (By similarity).
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3w68" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Ohto U]]
[[Category: Satow Y]]