pubmed-article:1970295 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C0008109 | lld:lifeskim |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:1970295 | lifeskim:mentions | umls-concept:C1710234 | lld:lifeskim |
pubmed-article:1970295 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:1970295 | pubmed:dateCreated | 1990-5-31 | lld:pubmed |
pubmed-article:1970295 | pubmed:abstractText | The molecular basis of ligand binding selectivity to beta-adrenergic receptor subtypes was investigated by designing chimeric beta 1/beta 2-adrenergic receptors. These molecules consisted of a set of reciprocal constructions, obtained by the exchange between the wild-type receptor genes of one to three unmodified transmembrane regions, together with their extracellular flanking regions. Eight different chimeras were expressed in Escherichia coli and studied with selective beta-adrenergic ligands. The evaluation of the relative effect of each chimeric exchange on ligand binding affinity was based on the analysis of delta G values, calculated from the equilibrium binding constants, as a function of the number of substituted beta 2-adrenergic receptor transmembrane domains. The data showed that the contribution of each exchanged region to subtype selectivity varies with each ligand; moreover, while several regions are critical for the pharmacological selectivity of all ligands, others are involved in the selectivity of only some compounds. The selectivity displayed by beta-adrenergic compounds towards beta 1 or beta 2 receptor subtypes thus results from a particular combination of interactions between each ligand and each of the subsites, variably distributed over the seven transmembrane regions of the receptor; these subsites are presumably defined by the individual structural properties of the ligands. | lld:pubmed |
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pubmed-article:1970295 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1970295 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1970295 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1970295 | pubmed:month | May | lld:pubmed |
pubmed-article:1970295 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:1970295 | pubmed:author | pubmed-author:StrosbergA... | lld:pubmed |
pubmed-article:1970295 | pubmed:author | pubmed-author:Delavier-Klut... | lld:pubmed |
pubmed-article:1970295 | pubmed:author | pubmed-author:MarulloSS | lld:pubmed |
pubmed-article:1970295 | pubmed:author | pubmed-author:EmorineL JLJ | lld:pubmed |
pubmed-article:1970295 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1970295 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:1970295 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1970295 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1970295 | pubmed:pagination | 1471-6 | lld:pubmed |
pubmed-article:1970295 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:1970295 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:1970295 | pubmed:articleTitle | Selective binding of ligands to beta 1, beta 2 or chimeric beta 1/beta 2-adrenergic receptors involves multiple subsites. | lld:pubmed |
pubmed-article:1970295 | pubmed:affiliation | Laboratoire de Biologie Moléculaire des Récepteurs, CNRS, Université Paris VII, Institut Pasteur, France. | lld:pubmed |
pubmed-article:1970295 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1970295 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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