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1oiz

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[[Image:1oiz.jpg|left|200px]]<br /><applet load="1oiz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oiz.jpg|left|200px]]
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caption="1oiz, resolution 1.88&Aring;" />
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'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''<br />
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{{Structure
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|PDB= 1oiz |SIZE=350|CAPTION= <scene name='initialview01'>1oiz</scene>, resolution 1.88&Aring;
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|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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|ACTIVITY=
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|GENE=
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}}
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'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''
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==Overview==
==Overview==
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==Disease==
==Disease==
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Known disease associated with this structure: Ataxia with isolated vitamin E deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600415 600415]]
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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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1OIZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=TRT:'>TRT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Trt+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIZ OCA].
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1OIZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIZ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12899840 12899840]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12899840 12899840]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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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 Feb 21 14:18:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:34 2008''

Revision as of 11:11, 20 March 2008

Image:1oiz.jpg


PDB ID 1oiz

Drag the structure with the mouse to rotate
, resolution 1.88Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN


Contents

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.

Disease

Known diseases associated with this structure: Ataxia with isolated vitamin E deficiency OMIM:[600415], Ceroid-lipofuscinosis, neuronal 2, classic late infantile OMIM:[607998]

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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