Source:http://linkedlifedata.com/resource/pubmed/id/12559765
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-1-31
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pubmed:abstractText |
The crystal structure of the glucocorticoid receptor (GR) ligand binding domain in a ternary complex with dexamethasone and a TIF2 coactivator peptide has been determined recently. The structure reveals several distinct features not found in other nuclear receptors, such as a novel dimerization interface and a second charge clamp that might be important in determining coactivator binding selectivity. The GR ligand binding domain also has a steroid binding pocket that is distinct from other nuclear receptors and might explain its selectivity for glucocorticoids and its diversity of responses.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0165-6147
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
58-61
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading | |
pubmed:year |
2003
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pubmed:articleTitle |
Crystallization of the human glucocorticoid receptor ligand binding domain: a step towards selective glucocorticoids.
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pubmed:affiliation |
Laboratory of Signal Transduction, Building 101, MD F3-07, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
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pubmed:publicationType |
Journal Article,
Review
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