1OIP

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

Summary for 1OIP

• Entry DOI: 10.2210/pdb1oip/pdb
• Related: 1OIZ 1R5L
• Descriptor: ALPHA-TOCOPHEROL TRANSFER PROTEIN, SULFATE ION, (2R)-2,5,7,8-TETRAMETHYL-2-[(4R,8R)-4,8,12-TRIMETHYLTRIDECYL]CHROMAN-6-OL, ... (4 entities in total)
• Functional Keywords: transport, ataxia, aved, transfer protein, tocopherol, vitamin e transport, disease mutation
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P49638
• Total number of polymer chains: 1
• Total formula weight: 32414.48

Authors

Meier, R.,Tomizaki, T.,Schulze-Briese, C.,Baumann, U.,Stocker, A. (deposition date: 2003-06-24, release date: 2004-01-14, Last modification date: 2011-07-13)

• Primary citation: Meier, R.,Tomizaki, T.,Schulze-Briese, C.,Baumann, U.,Stocker, A.; The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein; J.Mol.Biol., 331:725-, 2003; PubMed: 12899840; DOI: 10.1016/S0022-2836(03)00724-1

Experimental method

X-RAY DIFFRACTION (1.95 Å)