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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2004-2-17
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pubmed:abstractText |
A mutagenesis study to systematically analyse residues spanning the first extracellular loop of the GLP-1 receptor identified a double mutant, Met-204/Tyr-205-Ala/Ala, which displayed: markedly reduced affinity for the natural agonist GLP-1; slightly reduced affinity for its analogue exendin-4; and unaltered affinity for several N-terminally truncated analogues of GLP-1 and exendin-4. This suggests that the locus is important for the formation of the binding site for the N-terminal residues of peptide agonists.
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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/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Glucagon,
http://linkedlifedata.com/resource/pubmed/chemical/Glucagon-Like Peptide 1,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glucagon,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/exenatide,
http://linkedlifedata.com/resource/pubmed/chemical/glucagon-like peptide receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0929-8665
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14965274-Amino Acid Sequence,
pubmed-meshheading:14965274-Animals,
pubmed-meshheading:14965274-Cell Line,
pubmed-meshheading:14965274-Cyclic AMP,
pubmed-meshheading:14965274-Gene Expression Regulation,
pubmed-meshheading:14965274-Glucagon,
pubmed-meshheading:14965274-Glucagon-Like Peptide 1,
pubmed-meshheading:14965274-Humans,
pubmed-meshheading:14965274-Inhibitory Concentration 50,
pubmed-meshheading:14965274-Ligands,
pubmed-meshheading:14965274-Methionine,
pubmed-meshheading:14965274-Molecular Sequence Data,
pubmed-meshheading:14965274-Peptide Fragments,
pubmed-meshheading:14965274-Peptides,
pubmed-meshheading:14965274-Protein Precursors,
pubmed-meshheading:14965274-Rats,
pubmed-meshheading:14965274-Receptors, Glucagon,
pubmed-meshheading:14965274-Sequence Alignment,
pubmed-meshheading:14965274-Sequence Deletion,
pubmed-meshheading:14965274-Tyrosine,
pubmed-meshheading:14965274-Venoms
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pubmed:year |
2004
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pubmed:articleTitle |
Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues.
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pubmed:affiliation |
Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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