1olm
From Proteopedia
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| - | [[Image:1olm.jpg|left|200px]]<br /><applet load="1olm" size=" | + | [[Image:1olm.jpg|left|200px]]<br /><applet load="1olm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1olm, resolution 1.95Å" /> | caption="1olm, resolution 1.95Å" /> | ||
'''SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS'''<br /> | '''SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OLM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with VTQ as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Vtq Binding Site For Chain E'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1OLM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=VTQ:'>VTQ</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Vtq+Binding+Site+For+Chain+E'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:59:30 2008'' |
Revision as of 07:59, 3 February 2008
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SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS
Overview
The vast majority of monomeric lipid transport in nature is performed by, lipid-specific protein carriers. This class of proteins can enclose, cognate lipid molecules in a hydrophobic cavity and transport them across, the aqueous environment. Supernatant protein factor (SPF) is an enigmatic, representative of monomeric lipid transporters belonging to the SEC14, family. SPF stimulates squalene epoxidation, a downstream step of the, cholesterol biosynthetic pathway, by an unknown mechanism. Here, we, present the three-dimensional crystal structure of human SPF in complex, with RRR-alpha-tocopherylquinone, the major physiological oxidation, product of RRR-alpha-tocopherol, at a resolution of 1.95A. The structure, of the complex reveals how SPF sequesters RRR-alpha-tocopherylquinone, (RRR-alpha-TQ) in its protein body and permits a comparison with the, recently solved structure of human alpha-tocopherol transfer protein, (alpha-TTP) in complex with RRR-alpha-tocopherol. Recent findings have, shown that RRR-alpha-TQ is reduced in vivo to RRR-alpha-TQH(2), the latter, has been suggested to protect low-density lipoprotein (LDL) particles from, oxidation. Hence, the antioxidant function of the redox couple, RRR-alpha-TQ/RRR-alpha-TQH(2) in blocking LDL oxidation may reduce, cellular cholesterol uptake and thus explain how SPF upregulates, cholesterol synthesis.
About this Structure
1OLM is a Protein complex structure of sequences from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Supernatant protein factor in complex with RRR-alpha-tocopherylquinone: a link between oxidized Vitamin E and cholesterol biosynthesis., Stocker A, Baumann U, J Mol Biol. 2003 Sep 26;332(4):759-65. PMID:12972248
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