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Title: Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues. Author: López de Maturana R, Treece-Birch J, Abidi F, Findlay JB, Donnelly D. Journal: Protein Pept Lett; 2004 Feb; 11(1):15-22. PubMed ID: 14965274. 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.[Abstract] [Full Text] [Related] [New Search]