1xv9: Difference between revisions

Revision as of 06:17, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xv9.png

Template:STRUCTURE 1xv9

crystal structure of CAR/RXR heterodimer bound with SRC1 peptide, fatty acid, and 5b-pregnane-3,20-dione.crystal structure of CAR/RXR heterodimer bound with SRC1 peptide, fatty acid, and 5b-pregnane-3,20-dione.

Template:ABSTRACT PUBMED 15610735

About this StructureAbout this Structure

1XV9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer., Xu RX, Lambert MH, Wisely BB, Warren EN, Weinert EE, Waitt GM, Williams JD, Collins JL, Moore LB, Willson TM, Moore JT, Mol Cell. 2004 Dec 22;16(6):919-28. PMID:15610735

Page seeded by OCA on Mon Jul 28 06:17:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1xv9.gif|left|200px]]
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-'''crystal structure of CAR/RXR heterodimer bound with SRC1 peptide, fatty acid, and 5b-pregnane-3,20-dione.'''
+===crystal structure of CAR/RXR heterodimer bound with SRC1 peptide, fatty acid, and 5b-pregnane-3,20-dione.===
-==Overview==
+<!--
-The X-ray crystal structure of the human constitutive androstane receptor (CAR, NR1I3)/retinoid X receptor alpha (RXRalpha, NR2B1) heterodimer sheds light on the mechanism of ligand-independent activation of transcription by nuclear receptors. CAR contains a single-turn Helix X that restricts the conformational freedom of the C-terminal AF2 helix, favoring the active state of the receptor. Helix X and AF2 sit atop four amino acids that shield the CAR ligand binding pocket. A fatty acid ligand was identified in the RXRalpha binding pocket. The endogenous RXRalpha ligand, combined with stabilizing interactions from the heterodimer interface, served to hold RXRalpha in an active conformation. The structure suggests that upon translocation, CAR/RXRalpha heterodimers are preorganized in an active conformation in cells such that they can regulate transcription of target genes. Insights into the molecular basis of CAR constitutive activity can be exploited in the design of inverse agonists as drugs for treatment of obesity.
+The line below this paragraph, {{ABSTRACT_PUBMED_15610735}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15610735 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15610735}}
 ==About this Structure==
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 [[Category: Rxr]]
 [[Category: Src1]]
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