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1oiz

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[[Image:1oiz.jpg|left|200px]]
[[Image:1oiz.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1oiz |SIZE=350|CAPTION= <scene name='initialview01'>1oiz</scene>, resolution 1.88&Aring;
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The line below this paragraph, containing "STRUCTURE_1oiz", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Trt+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1oiz| PDB=1oiz | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oiz OCA], [http://www.ebi.ac.uk/pdbsum/1oiz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oiz RCSB]</span>
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}}
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'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''
'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''
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[[Category: Stocker, A.]]
[[Category: Stocker, A.]]
[[Category: Tomizaki, T.]]
[[Category: Tomizaki, T.]]
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[[Category: ataxia]]
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[[Category: Ataxia]]
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[[Category: aved]]
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[[Category: Aved]]
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[[Category: tocopherol]]
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[[Category: Tocopherol]]
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[[Category: transfer protein]]
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[[Category: Transfer protein]]
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[[Category: transport]]
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[[Category: Transport]]
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[[Category: vitamin e]]
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[[Category: Vitamin e]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:54:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:01 2008''
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Revision as of 00:54, 3 May 2008

Image:1oiz.jpg

Template:STRUCTURE 1oiz

THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN


Overview

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.

About this Structure

1OIZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 03:54:40 2008

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