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1oiz
From Proteopedia
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|PDB= 1oiz |SIZE=350|CAPTION= <scene name='initialview01'>1oiz</scene>, resolution 1.88Å | |PDB= 1oiz |SIZE=350|CAPTION= <scene name='initialview01'>1oiz</scene>, resolution 1.88Å | ||
|SITE= <scene name='pdbsite=AC1:Trt+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Trt+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=TRT:FRAGMENT OF TRITON X-100'>TRT</scene> | + | |LIGAND= <scene name='pdbligand=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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==Overview== | ==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. | 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 diseases associated with this structure: Ataxia with isolated vitamin E deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600415 600415]], Ceroid-lipofuscinosis, neuronal 2, classic late infantile OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607998 607998]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Stocker, A.]] | [[Category: Stocker, A.]] | ||
[[Category: Tomizaki, T.]] | [[Category: Tomizaki, T.]] | ||
| - | [[Category: TRT]] | ||
[[Category: ataxia]] | [[Category: ataxia]] | ||
[[Category: aved]] | [[Category: aved]] | ||
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[[Category: vitamin e]] | [[Category: vitamin e]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:01 2008'' |
Revision as of 19:46, 30 March 2008
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| , resolution 1.88Å | |||||||
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| Sites: | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:46:01 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
