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1oiz
From Proteopedia
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[[Image:1oiz.jpg|left|200px]] | [[Image:1oiz.jpg|left|200px]] | ||
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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.]] | ||
| - | [[Category: | + | [[Category: Ataxia]] |
| - | [[Category: | + | [[Category: Aved]] |
| - | [[Category: | + | [[Category: Tocopherol]] |
| - | [[Category: | + | [[Category: Transfer protein]] |
| - | [[Category: | + | [[Category: Transport]] |
| - | [[Category: | + | [[Category: Vitamin e]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:54:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:54, 3 May 2008
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
Categories: Homo sapiens | Single protein | Baumann, U. | Meier, R. | Schulze-Briese, C. | Stocker, A. | Tomizaki, T. | Ataxia | Aved | Tocopherol | Transfer protein | Transport | Vitamin e
