1oiz

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|PDB= 1oiz |SIZE=350|CAPTION= <scene name='initialview01'>1oiz</scene>, resolution 1.88&Aring;
|PDB= 1oiz |SIZE=350|CAPTION= <scene name='initialview01'>1oiz</scene>, resolution 1.88&Aring;
|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>
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|LIGAND= <scene name='pdbligand=TRT:FRAGMENT OF TRITON X-100'>TRT</scene>
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|LIGAND= <scene name='pdbligand=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|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.
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==Disease==
 
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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.]]
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[[Category: TRT]]
 
[[Category: ataxia]]
[[Category: ataxia]]
[[Category: aved]]
[[Category: aved]]
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[[Category: vitamin e]]
[[Category: vitamin e]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:34 2008''
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''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

Image:1oiz.jpg


PDB ID 1oiz

Drag the structure with the mouse to rotate
, resolution 1.88Å
Sites:
Ligands:
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

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