| pubmed-article:8816747 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8816747 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:8816747 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
| pubmed-article:8816747 | lifeskim:mentions | umls-concept:C0034787 | lld:lifeskim |
| pubmed-article:8816747 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:8816747 | lifeskim:mentions | umls-concept:C1412113 | lld:lifeskim |
| pubmed-article:8816747 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8816747 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8816747 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:8816747 | pubmed:dateCreated | 1996-11-13 | lld:pubmed |
| pubmed-article:8816747 | pubmed:abstractText | The coupling of agonist-activated seven transmembrane domain receptors to G proteins is known to involve the amino-terminal region of their third cytoplasmic loop. Analysis of the amino acids in this region of the rat type in angiotensin (AT1a) receptor identified Leu-222 as an essential residue in receptor activation by the physiological agonist, angiotensin II (Ang II). Nonpolar replacements for Leu-222 yielded functionally intact AT1 receptors, while polar or charged residues caused progressive impairment of Ang II-induced inositol phosphate generation. The decrease in agonist-induced signal generation was associated with a parallel reduction of receptor internalization, and was most pronounced for the Lys-222 mutant receptor. Although this mutant showed normal binding of the peptide antagonist, [Sar1,Ile6]Ang II, its affinity for Ang II was markedly reduced, consistent with its inability to adopt the high-affinity conformation. A search revealed that many Gq-coupled receptors contain an apolar amino acid (frequently leucine) in the position corresponding to Leu-222 of the AT1 receptor. These findings suggest that such a conserved apolar residue in the third intracellular loop is a crucial element in the agonist-induced activation of the AT1 and possibly many other G protein-coupled receptors. | lld:pubmed |
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| pubmed-article:8816747 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8816747 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8816747 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8816747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8816747 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8816747 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8816747 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8816747 | pubmed:author | pubmed-author:CattK JKJ | lld:pubmed |
| pubmed-article:8816747 | pubmed:author | pubmed-author:JagadeeshGG | lld:pubmed |
| pubmed-article:8816747 | pubmed:author | pubmed-author:BallaTT | lld:pubmed |
| pubmed-article:8816747 | pubmed:author | pubmed-author:BoxCC | lld:pubmed |
| pubmed-article:8816747 | pubmed:author | pubmed-author:ZhangMM | lld:pubmed |
| pubmed-article:8816747 | pubmed:author | pubmed-author:HunyadyLL | lld:pubmed |
| pubmed-article:8816747 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8816747 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:8816747 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8816747 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8816747 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8816747 | pubmed:pagination | 10040-5 | lld:pubmed |
| pubmed-article:8816747 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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