Abstract
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.
Keywords: Met-204 And Tyr-205, N-terminally, Glp-1 Receptor
Protein & Peptide Letters
Title: Met-204 And Tyr-205 Are Together Important For Binding Glp-1 Receptor Agonists But Not Their N-Terminally Truncated Analogues
Volume: 11 Issue: 1
Author(s): Rakel Lopez de Maturana, Janet Treece-Birch, Fatima Abidi, John B.C. Findlay and Dan Donnelly
Affiliation:
Keywords: Met-204 And Tyr-205, N-terminally, Glp-1 Receptor
Abstract: 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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Cite this article as:
de Maturana Lopez Rakel, Treece-Birch Janet, Abidi Fatima, Findlay B.C. John and Donnelly Dan, Met-204 And Tyr-205 Are Together Important For Binding Glp-1 Receptor Agonists But Not Their N-Terminally Truncated Analogues, Protein & Peptide Letters 2004; 11 (1) . https://dx.doi.org/10.2174/0929866043478491
DOI https://dx.doi.org/10.2174/0929866043478491 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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