Moon, Mi JinLee, Yoo-NaPark, SumiReyes-Alcaraz, ArfaxadHwang, Jong-IkMillar, Robert P.Choe, HanSeong, Jae Young2015-12-142015-02Moon, MJ, Lee, Y-N, Park, S, Reyes-Alcaraz, A, Hwang, J-I, Millar, RP, Choe, H & Seong, JY 2015, 'Ligand binding pocket formed by evolutionarily conserved residues in the glucagon-like peptide-1 (GLP-1) receptor core domain', Journal of Biological Chemistry, vol. 290, no. 9, pp. 5696-5706.0021-9258 (print)1083-351X (online)10.1074/jbc.M114.612606http://hdl.handle.net/2263/51181BACKGROUND : Little is known about the interaction between GLP-1 and the heptahelical core domain of GLP1R. RESULTS : GLP-1 Asp9 and Gly4 interact with the evolutionarily conserved residues in extracellular loop 3. CONCLUSION : Ligand binding pocket formed by evolutionarily conserved residues in the GLP1R core domain. Significance: This study highlights the mechanism underlying high affinity interaction between GLP-1 and the binding pocket of the receptor.en© 2015 by The American Society for Biochemistry and Molecular Biology, Inc. This research was originally published in Journal of Biological Chemistry. Moon, MJ, Lee, Y-N, Park, S, Reyes-Alcaraz, A, Hwang, J-I, Millar, RP, Choe, H & Seong, JY, Ligand binding pocket formed by evolutionarily conserved residues in the glucagon-like peptide-1 (GLP-1) receptor core domain, 2015, vol. 290, no. 9, pp. 5696–5706, doi : 10.1074/jbc.M114.612606 .Glucagon-like peptide-1 (GLP-1)Molecular mechanismInteractionLigand binding pocketPostprint Article