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The molecular basis of vitamin E retention: structure of human alpha-tocopherol transfer protein.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Meier R,Tomizaki T,Schulze-Briese C,Baumann U,Stocker A

doi

10.1016/s0022-2836(03)00724-1

keywords:

subject

Has Abstract

pub_date

2003-08-15 00:00:00

pages

725-34

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022283603007241

journal_volume

331

pub_type

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