Source:http://linkedlifedata.com/resource/pubmed/id/17123625
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-1-29
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pubmed:abstractText |
Thyrotropin-releasing hormone (TRH), a tripeptide, exerts its biological effects through stimulation of cell-surface receptors, TRH-R, belonging to the superfamily of G protein-coupled receptors (GPCR). Because of the intermediate size of TRH, it is smaller than polypeptide ligands that interact at GPCR ectodomains and larger than biogenic amines, which interact within GPCR transmembrane domains (TMD), the TRH/TRH-R complex probably shares properties of these 2 extremes, representing a unique system to study GPCR/ligand interactions. In this review, we summarize the current knowledge of the structure-activity relationships in the TRH/TRH-R system. Based on experimental data and the structural information acquired from computer simulations, we formulate a working hypothesis to describe the molecular events underlying the processes of TRH binding and TRH-R activation. This hypothesis represents a starting point for understanding the biology of the TRH/TRH-R system on a molecular level and provides a basis for potential design of new potent and selective modulators of TRH-R's activity.
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pubmed:grant | |
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 |
0163-7258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
113
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
410-9
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pubmed:dateRevised |
2008-4-16
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pubmed:meshHeading |
pubmed-meshheading:17123625-Animals,
pubmed-meshheading:17123625-Binding Sites,
pubmed-meshheading:17123625-Models, Molecular,
pubmed-meshheading:17123625-Protein Conformation,
pubmed-meshheading:17123625-Receptors, Thyrotropin-Releasing Hormone,
pubmed-meshheading:17123625-Thyrotropin-Releasing Hormone
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pubmed:year |
2007
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pubmed:articleTitle |
Thyrotropin-releasing hormone and its receptors--a hypothesis for binding and receptor activation.
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pubmed:affiliation |
Clinical Endocrinology Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, N.I.H., Intramural
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