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1oip

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[[Image:1oip.jpg|left|200px]]<br /><applet load="1oip" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oip, resolution 1.95&Aring;" />
 
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'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''<br />
 
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==Overview==
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==The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein==
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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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<StructureSection load='1oip' size='340' side='right'caption='[[1oip]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oip]] is a 1 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=1OIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OIP 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]] 1.95&#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=SO4:SULFATE+ION'>SO4</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>
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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=1oip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oip OCA], [https://pdbe.org/1oip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oip RCSB], [https://www.ebi.ac.uk/pdbsum/1oip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oip 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/1oip_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1oip 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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==Disease==
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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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Known disease associated with this structure: Ataxia with isolated vitamin E deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600415 600415]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1OIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and VIV as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Vit Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OIP OCA].
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</div>
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<div class="pdbe-citations 1oip" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12899840 12899840]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baumann, U.]]
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[[Category: Baumann U]]
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[[Category: Meier, R.]]
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[[Category: Meier R]]
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[[Category: Schulze-Briese, C.]]
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[[Category: Schulze-Briese C]]
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[[Category: Stocker, A.]]
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[[Category: Stocker A]]
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[[Category: Tomizaki, T.]]
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[[Category: Tomizaki T]]
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[[Category: SO4]]
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[[Category: VIV]]
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[[Category: ataxia]]
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[[Category: aved]]
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[[Category: disease mutation]]
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[[Category: tocopherol]]
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[[Category: transfer protein]]
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[[Category: vitamin e transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:45:48 2007''
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Current revision

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

PDB ID 1oip

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