| pubmed-article:17381074 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C0034791 | lld:lifeskim |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:17381074 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:17381074 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:17381074 | pubmed:dateCreated | 2007-4-10 | lld:pubmed |
| pubmed-article:17381074 | pubmed:abstractText | Activation of guanine nucleotide-binding protein (G protein)-coupled receptors is believed to involve conformational change that exposes a domain for G protein coupling at the cytosolic surface of the helical confluence, although the mechanisms for achieving this are not well understood. This conformational change can be achieved by docking a diverse variety of agonist ligands, known to occur by interacting with different regions of these receptors. In this study, we focus on the importance of a specific basic residue (Lys187) within the second extracellular loop of the receptor for the peptide hormone, cholecystokinin. Alanine-replacement and charge-reversal mutagenesis of this residue showed that it had no effect on the binding of natural peptide and nonpeptidyl ligands of this receptor but markedly interfered with agonist-stimulated signaling. It was demonstrated that this negative effect on biological activity could be eliminated with the truncation of the first 30 residues of the amino-terminal tail of this receptor. Complementary charge-reversal mutagenesis of each of the five conserved acidic residues within this region of the receptor in the presence of the charge-reversed Lys187 revealed that only the Asp5 mutant fully reversed the negative functional impact of the Lys187 charge reversal. Thus, we have demonstrated that a basic residue within the second extracellular loop of the cholecystokinin receptor interacts with a specific acidic residue within the amino terminus of this receptor. This residue-residue interaction is nicely accommodated within a new molecular model of the agonist-occupied cholecystokinin receptor. | lld:pubmed |
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| pubmed-article:17381074 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17381074 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17381074 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17381074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17381074 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17381074 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17381074 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:17381074 | pubmed:author | pubmed-author:BøeH AHA | lld:pubmed |
| pubmed-article:17381074 | pubmed:author | pubmed-author:MillerLaurenc... | lld:pubmed |
| pubmed-article:17381074 | pubmed:author | pubmed-author:DongMaoqingM | lld:pubmed |
| pubmed-article:17381074 | pubmed:author | pubmed-author:AbagyanRubenR | lld:pubmed |
| pubmed-article:17381074 | pubmed:author | pubmed-author:DingXi-QinXQ | lld:pubmed |
| pubmed-article:17381074 | pubmed:author | pubmed-author:LamPolo C-HPC | lld:pubmed |
| pubmed-article:17381074 | pubmed:author | pubmed-author:ThomasScott... | lld:pubmed |
| pubmed-article:17381074 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17381074 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:17381074 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:17381074 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17381074 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17381074 | pubmed:pagination | 4522-31 | lld:pubmed |
| pubmed-article:17381074 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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| pubmed-article:17381074 | pubmed:meshHeading | pubmed-meshheading:17381074... | lld:pubmed |
| pubmed-article:17381074 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17381074 | pubmed:articleTitle | Role of lysine187 within the second extracellular loop of the type A cholecystokinin receptor in agonist-induced activation. Use of complementary charge-reversal mutagenesis to define a functionally important interdomain interaction. | lld:pubmed |
| pubmed-article:17381074 | pubmed:affiliation | Cancer Center and Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Scottsdale, Arizona 85259, USA. | lld:pubmed |
| pubmed-article:17381074 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17381074 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17381074 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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