Structural and molecular conservation of glucagon-like peptide-1 and its receptor confers selective ligand-receptor interaction
DC Field | Value | Language |
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dc.contributor.author | Moon, M.J. | - |
dc.contributor.author | Park, S. | - |
dc.contributor.author | Kim, D.-K. | - |
dc.contributor.author | Cho, E.B. | - |
dc.contributor.author | Hwang, J.-I. | - |
dc.contributor.author | Vaudry, H. | - |
dc.contributor.author | Seong, J.Y. | - |
dc.date.accessioned | 2021-09-07T04:03:51Z | - |
dc.date.available | 2021-09-07T04:03:51Z | - |
dc.date.created | 2021-06-17 | - |
dc.date.issued | 2012 | - |
dc.identifier.issn | 1664-2392 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/110612 | - |
dc.description.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. © 2012 Moon, Park, Kim, Cho, Hwang, Vaudry and Seong. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.title | Structural and molecular conservation of glucagon-like peptide-1 and its receptor confers selective ligand-receptor interaction | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Seong, J.Y. | - |
dc.identifier.doi | 10.3389/fendo.2012.00141 | - |
dc.identifier.scopusid | 2-s2.0-84874415937 | - |
dc.identifier.bibliographicCitation | Frontiers in Endocrinology, v.3, no.NOV | - |
dc.relation.isPartOf | Frontiers in Endocrinology | - |
dc.citation.title | Frontiers in Endocrinology | - |
dc.citation.volume | 3 | - |
dc.citation.number | NOV | - |
dc.type.rims | ART | - |
dc.type.docType | Review | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Evolution | - |
dc.subject.keywordAuthor | G protein-coupled receptors | - |
dc.subject.keywordAuthor | GLP-1 | - |
dc.subject.keywordAuthor | GLP1R | - |
dc.subject.keywordAuthor | Ligand-receptor interaction | - |
dc.subject.keywordAuthor | Ortholog | - |
dc.subject.keywordAuthor | Paralog | - |
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