Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues.

Rakel López de Maturana, Janet Treece-Birch, Fatima Abidi, John B C Findlay, Dan Donnelly

Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.

Protein and peptide letters 2004 Feb

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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.

Citation

Rakel López de Maturana, Janet Treece-Birch, Fatima Abidi, John B C Findlay, Dan Donnelly. Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues. Protein and peptide letters. 2004 Feb;11(1):15-22