Title |
Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction
|
---|---|
Published in |
Frontiers in endocrinology, January 2012
|
DOI | 10.3389/fendo.2012.00141 |
Pubmed ID | |
Authors |
Mi Jin Moon, Sumi Park, Dong-Kyu Kim, Eun Bee Cho, Jong-Ik Hwang, Hubert Vaudry, Jae Young Seong |
Abstract |
Glucagon-like peptide-1 (GLP-1) is a major player in the regulation of glucose homeostasis. It acts on pancreatic beta cells to stimulate insulin secretion and on the brain to inhibit appetite. Thus, it may be a promising therapeutic agent for the treatment of type 2 diabetes mellitus and obesity. Despite the physiological and clinical importance of GLP-1, molecular interaction with the GLP-1 receptor (GLP1R) is not well understood. Particularly, the specific amino acid residues within the transmembrane helices and extracellular loops of the receptor that may confer ligand-induced receptor activation have been poorly investigated. Amino acid sequence comparisons of GLP-1 and GLP1R with their orthologs and paralogs in vertebrates, combined with biochemical approaches, are useful to determine which amino acid residues in the peptide and the receptor confer selective ligand-receptor interaction. This article reviews how the molecular evolution of GLP-1 and GLP1R contributes to the selective interaction between this ligand-receptor pair, providing critical clues for the development of potent agonists for the treatment of diabetes mellitus and obesity. |
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