1oiz

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[[Image:1oiz.png|left|200px]]
 
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{{STRUCTURE_1oiz| PDB=1oiz | SCENE= }}
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==The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein==
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<StructureSection load='1oiz' size='340' side='right'caption='[[1oiz]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oiz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OIZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oiz OCA], [https://pdbe.org/1oiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oiz RCSB], [https://www.ebi.ac.uk/pdbsum/1oiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oiz ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/TTPA_HUMAN TTPA_HUMAN] Defects in TTPA are the cause of ataxia with isolated vitamin E deficiency (AVED) [MIM:[https://omim.org/entry/277460 277460]. AVED is an autosomal recessive disease characterized by spinocerebellar degeneration. It causes ataxia and peripheral neuropathy that resembles Friedreich ataxia. AVED patients have markedly reduced plasma levels of vitamin E.<ref>PMID:8602747</ref> <ref>PMID:9463307</ref> <ref>PMID:7719340</ref> <ref>PMID:7566022</ref> <ref>PMID:15065857</ref> <ref>PMID:15300460</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/TTPA_HUMAN TTPA_HUMAN] Binds alpha-tocopherol and enhances its transfer between separate membranes.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oi/1oiz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oiz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Alpha-tocopherol transfer protein (alpha-TTP) is a liver protein responsible for the selective retention of alpha-tocopherol from dietary vitamin E, which is a mixture of alpha, beta, gamma, and delta-tocopherols and the corresponding tocotrienols. The alpha-TTP-mediated transfer of alpha-tocopherol into nascent VLDL is the major determinant of plasma alpha-tocopherol levels in humans. Mutations in the alpha-TTP gene have been detected in patients suffering from low plasma alpha-tocopherol and ataxia with isolated vitamin E deficiency (AVED). The crystal structure of alpha-TTP reveals two conformations. In its closed tocopherol-charged form, a mobile helical surface segment seals the hydrophobic binding pocket. In the presence of detergents, an open conformation is observed, which probably represents the membrane-bound form. The selectivity of alpha-TTP for RRR-alpha-tocopherol is explained from the van der Waals contacts occurring in the lipid-binding pocket. Mapping the known mutations leading to AVED onto the crystal structure shows that no mutations occur directly in the binding pocket.
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===THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN===
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The molecular basis of vitamin E retention: structure of human alpha-tocopherol transfer protein.,Meier R, Tomizaki T, Schulze-Briese C, Baumann U, Stocker A J Mol Biol. 2003 Aug 15;331(3):725-34. PMID:12899840<ref>PMID:12899840</ref>
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{{ABSTRACT_PUBMED_12899840}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1oiz" style="background-color:#fffaf0;"></div>
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[[1oiz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIZ OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:012899840</ref><references group="xtra"/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Baumann, U.]]
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[[Category: Large Structures]]
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[[Category: Meier, R.]]
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[[Category: Baumann U]]
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[[Category: Schulze-Briese, C.]]
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[[Category: Meier R]]
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[[Category: Stocker, A.]]
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[[Category: Schulze-Briese C]]
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[[Category: Tomizaki, T.]]
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[[Category: Stocker A]]
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[[Category: Ataxia]]
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[[Category: Tomizaki T]]
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[[Category: Aved]]
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[[Category: Tocopherol]]
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[[Category: Transfer protein]]
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[[Category: Transport]]
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[[Category: Vitamin e]]
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Current revision

The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein

PDB ID 1oiz

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