Ligand binding pocket formed by evolutionarily conserved residues in the glucagon-like peptide-1 (GLP-1) receptor core domain

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Authors

Moon, Mi Jin
Lee, Yoo-Na
Park, Sumi
Reyes-Alcaraz, Arfaxad
Hwang, Jong-Ik
Millar, Robert P.
Choe, Han
Seong, Jae Young

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Publisher

American Society for Biochemistry and Molecular Biology

Abstract

BACKGROUND : 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.

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Keywords

Glucagon-like peptide-1 (GLP-1), Molecular mechanism, Interaction, Ligand binding pocket

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Citation

Moon, 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.