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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1998-9-3
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pubmed:databankReference | |
pubmed:abstractText |
The retinoid X receptor (RXR) is a member of the nuclear hormone receptor superfamily of transcriptional regulators and plays a central role in the retinoid and, through its ability to heterodimerize with other nuclear hormone receptors, non-steroid signaling pathways. The DNA-binding and recognition functions of RXR are located in a conserved 83 amino acid residue domain that recognizes the consensus sequence AGGTCA. In order to provide a detailed picture of its structure, we have calculated a high-resolution solution structure of the C195A RXRalpha DNA-binding domain. Structures were calculated using 1131 distance and dihedral angle constraints derived from 1H, 13C and 15N NMR spectra. The structures reveal a perpendicularly packed, "loop-helix" fold similar to other nuclear hormone receptor DNA-binding domains and confirm the existence of the C-terminal helix, which was first observed in the low-resolution NMR structure. The C-terminal helix is well formed and is stabilized by packing interactions with residues in the hydrophobic core. The solution structure of RXR is very similar to that determined by X-ray crystallographic studies of the RXR-TR heterodimer complex with DNA, except that in the latter case no electron density was observed for residues corresponding to the C-terminal helix. Other differences between the X-ray and NMR structures occur in the second zinc-binding loop, which is disordered in solution. Heteronuclear 15N NOE measurements suggest that this loop has enhanced flexibility in the free protein.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1998 Academic Press
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
271-84
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9698548-Amino Acid Sequence,
pubmed-meshheading:9698548-Binding Sites,
pubmed-meshheading:9698548-Crystallography, X-Ray,
pubmed-meshheading:9698548-DNA,
pubmed-meshheading:9698548-Humans,
pubmed-meshheading:9698548-Models, Molecular,
pubmed-meshheading:9698548-Molecular Sequence Data,
pubmed-meshheading:9698548-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9698548-Protein Structure, Secondary,
pubmed-meshheading:9698548-Receptors, Retinoic Acid,
pubmed-meshheading:9698548-Retinoid X Receptors,
pubmed-meshheading:9698548-Transcription Factors,
pubmed-meshheading:9698548-Zinc
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pubmed:year |
1998
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pubmed:articleTitle |
High-resolution solution structure of the retinoid X receptor DNA-binding domain.
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pubmed:affiliation |
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla,, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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