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1upv
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(New page: 200px<br /> <applet load="1upv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1upv, resolution 2.10Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 18:25, 29 October 2007
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CRYSTAL STRUCTURE OF THE HUMAN LIVER X RECEPTOR BETA LIGAND BINDING DOMAIN IN COMPLEX WITH A SYNTHETIC AGONIST
Overview
LXRbeta belongs to the nuclear hormone receptor superfamily of, ligand-activated transcription factors. Its natural ligands are supposed, to be oxidised derivatives of cholesterol. Stimulation of LXRbeta by, agonists activates a number of genes that are involved in the regulation, of lipid metabolism and cholesterol efflux from cells. Therefore, LXRbeta, may represent a novel therapeutic target for the treatment of dyslipidemia, and atherosclerosis.Here, we report the X-ray crystal structure of the, LXRbeta ligand-binding domain in complex with a synthetic agonist, T-0901317. This compound occupies the ligand-binding pocket of the, receptor, forms numerous lipophilic contacts with the protein and one, crucial hydrogen bond to His435 and stabilises the agonist conformation of, the receptor ... [(full description)]
About this Structure
1UPV is a [Single protein] structure of sequence from [Homo sapiens] with 444 as [ligand]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the human liver X receptor beta ligand-binding domain in complex with a synthetic agonist., Hoerer S, Schmid A, Heckel A, Budzinski RM, Nar H, J Mol Biol. 2003 Dec 12;334(5):853-61. PMID:14643652
Page seeded by OCA on Mon Oct 29 20:29:42 2007
