Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction

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. D...

Full description

Bibliographic Details
Main Authors:	Moon, Mi Jin, Park, Sumi, Kim, Dong-Kyu, Cho, Eun Bee, Hwang, Jong-Ik, Vaudry, Hubert, Seong, Jae Young
Format:	Online
Language:	English
Published:	Frontiers Media S.A. 2012
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3500760/

id	pubmed-3500760
recordtype	oai_dc
spelling	pubmed-35007602012-11-23 Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction Moon, Mi Jin Park, Sumi Kim, Dong-Kyu Cho, Eun Bee Hwang, Jong-Ik Vaudry, Hubert Seong, Jae Young Endocrinology 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. Frontiers Media S.A. 2012-11-19 /pmc/articles/PMC3500760/ /pubmed/23181056 http://dx.doi.org/10.3389/fendo.2012.00141 Text en Copyright © 2012 Moon, Park, Kim, Cho, Hwang, Vaudry and Seong. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Moon, Mi Jin Park, Sumi Kim, Dong-Kyu Cho, Eun Bee Hwang, Jong-Ik Vaudry, Hubert Seong, Jae Young
spellingShingle	Moon, Mi Jin Park, Sumi Kim, Dong-Kyu Cho, Eun Bee Hwang, Jong-Ik Vaudry, Hubert Seong, Jae Young Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction
author_facet	Moon, Mi Jin Park, Sumi Kim, Dong-Kyu Cho, Eun Bee Hwang, Jong-Ik Vaudry, Hubert Seong, Jae Young
author_sort	Moon, Mi Jin
title	Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction
title_short	Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction
title_full	Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction
title_fullStr	Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction
title_full_unstemmed	Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction
title_sort	structural and molecular conservation of glucagon-like peptide-1 and its receptor confers selective ligand-receptor interaction
description	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.
publisher	Frontiers Media S.A.
publishDate	2012
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3500760/
_version_	1611925015219929088

Structural and Molecular Conservation of Glucagon-Like Peptide-1 and Its Receptor Confers Selective Ligand-Receptor Interaction

Similar Items