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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2003-3-7
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pubmed:abstractText |
A urotensin II (U-II) peptide analogue containing the photoreactive p -benzoyl-L-phenylalanine (Bz-Phe) in the sixth position was used to identify ligand-binding sites of the rat U-II receptor, also known as GPR14. [Bz-Phe(6)]U-II bound the receptor expressed in COS-7 cells with high affinity (IC(50) 0.7 nM) and was as potent as U-II in the agonist-induced production of inositol phosphate. Photolabelling of the U-II receptor with (125)I-[Bz-Phe(6)]U-II resulted in the specific formation of a glycosylated (125)I-[Bz-Phe(6)]U-II-U-II receptor complex of 60 kDa. Digestion of the 60 kDa complex with endoproteinase Glu-C generated a fragment of 17 kDa circumscribing the labelled fragment to residues 148-286. Digestion of the ligand-receptor complex with endoproteinase Arg-C produced a short peptide of 4 kDa corresponding to fragments 125-148, 167-192 or 210-233. CNBr treatment of the endoproteinase-Glu-C and -Arg-C fragments yielded 2 kDa fragments, defining the labelling site to methionine residues 184/185 of the fourth transmembrane domain. Photolabelling of two mutant receptors, M184L/M185L and M184A/M185A, led to a significant decrease in the overall yield of covalent labelling. Taken together, our results indicate that position 6 of U-II normally occupied by phenylalanine would interact with Met(184) and/or Met(185) of the fourth transmembrane domain of the U-II receptor. This information should be of significant value in the study of the interactions between U-II and its cognate receptor.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10194764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10393537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10486557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10499587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10548501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10559967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10617579,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-10807654,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-9079697,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12495432-9880548
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide-N4-(N-acetyl-beta-glucosamin...,
http://linkedlifedata.com/resource/pubmed/chemical/Photoaffinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Urotensins,
http://linkedlifedata.com/resource/pubmed/chemical/Uts2r protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/urotensin II
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
370
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
829-38
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12495432-Amidohydrolases,
pubmed-meshheading:12495432-Amino Acid Sequence,
pubmed-meshheading:12495432-Animals,
pubmed-meshheading:12495432-Binding Sites,
pubmed-meshheading:12495432-COS Cells,
pubmed-meshheading:12495432-Endopeptidases,
pubmed-meshheading:12495432-Humans,
pubmed-meshheading:12495432-Ligands,
pubmed-meshheading:12495432-Molecular Sequence Data,
pubmed-meshheading:12495432-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase,
pubmed-meshheading:12495432-Photoaffinity Labels,
pubmed-meshheading:12495432-Protein Binding,
pubmed-meshheading:12495432-Protein Isoforms,
pubmed-meshheading:12495432-Protein Structure, Secondary,
pubmed-meshheading:12495432-Protein Structure, Tertiary,
pubmed-meshheading:12495432-Rats,
pubmed-meshheading:12495432-Receptors, Cell Surface,
pubmed-meshheading:12495432-Receptors, G-Protein-Coupled,
pubmed-meshheading:12495432-Urotensins
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pubmed:year |
2003
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pubmed:articleTitle |
Photolabelling the rat urotensin II/GPR14 receptor identifies a ligand-binding site in the fourth transmembrane domain.
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pubmed:affiliation |
Department of Pharmacology, Faculty of Medicine, Université de Sherbrooke, Sherbrooke, Québec, Canada J1H 5N4.
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