1oip
From Proteopedia
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| - | [[Image:1oip.jpg|left|200px]]<br /><applet load="1oip" size=" | + | [[Image:1oip.jpg|left|200px]]<br /><applet load="1oip" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oip, resolution 1.95Å" /> | caption="1oip, resolution 1.95Å" /> | ||
'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''<br /> | '''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=VIV:'>VIV</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vitamin e transport]] | [[Category: vitamin e transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:58:37 2008'' |
Revision as of 07:58, 3 February 2008
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THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN
Contents |
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.
Disease
Known disease associated with this structure: Ataxia with isolated vitamin E deficiency OMIM:[600415]
About this Structure
1OIP is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Site: . 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 Sun Feb 3 09:58:37 2008
Categories: Homo sapiens | Single protein | Baumann, U. | Meier, R. | Schulze-Briese, C. | Stocker, A. | Tomizaki, T. | SO4 | VIV | Ataxia | Aved | Disease mutation | Tocopherol | Transfer protein | Vitamin e transport
