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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Seong, Jae Young Hwang, Jong-ik Millar, Robert Peter Choe, Han Park, Sumi Reyes-alcaraz, Arfaxad Moon, Mi Jin Lee, Yoo-na |
| Description | Author Affiliation: Moon MJ ( From the Graduate School of Medicine, Korea University, Seoul 136-705, Republic of Korea.); Lee YN ( From the Graduate School of Medicine, Korea University, Seoul 136-705, Republic of Korea.); Park S ( From the Graduate School of Medicine, Korea University, Seoul 136-705, Republic of Korea.); Reyes-Alcaraz A ( From the Graduate School of Medicine, Korea University, Seoul 136-705, Republic of Korea.); Hwang JI ( From the Graduate School of Medicine, Korea University, Seoul 136-705, Republic of Korea.); Millar RP ( Mammal Research Institute, Department of Zoology and Entomology, University of Pretoria, Pretoria 0028, Medical Research Council Receptor Biology Unit, and University of Cape Town, Cape Town 7925, South Africa, and Centre for Integrative Physiology, University of Edinburgh, Edinburgh EH164TJ, Scotla); Choe H ( Department of Physiology and Bio-Medical Institute of Technology, University of Ulsan College of Medicine, Seoul 138-736, Korea hchoe@ulsan.ac.kr.); Seong JY ( From the Graduate School of Medicine, Korea University, Seoul 136-705, Republic of Korea, jyseong@korea.ac.kr.) |
| Abstract | Glucagon-like peptide-1 (GLP-1) plays a pivotal role in glucose homeostasis through its receptor GLP1R. Due to its multiple beneficial effects, GLP-1 has gained great attention for treatment of type 2 diabetes and obesity. However, little is known about the molecular mechanism underlying the interaction of GLP-1 with the heptahelical core domain of GLP1R conferring high affinity ligand binding and ligand-induced receptor activation. Here, using chimeric and point-mutated GLP1R, we determined that the evolutionarily conserved amino acid residue Arg(380) flanked by hydrophobic Leu(379) and Phe(381) in extracellular loop 3 (ECL3) may have an interaction with Asp(9) and Gly(4) of the GLP-1 peptide. The molecular modeling study showed that Ile(196) at transmembrane helix 2, Met(233) at ECL1, and Asn(302) at ECL2 of GLP1R have contacts with His(1) and Thr(7) of GLP-1. This study may shed light on the mechanism underlying high affinity interaction between the ligand and the binding pocket that is formed by these conserved residues in the GLP1R core domain. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 9 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-02-27 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amino Acids Chemistry Glucagon-Like Peptide 1 Protein Structure, Tertiary Receptors, Glucagon Amino Acid Sequence Genetics Metabolism Binding Sites Conserved Sequence Evolution, Molecular Glucagon-Like Peptide-1 Receptor HEK293 Cells Ligands Models, Molecular Molecular Sequence Data Peptides Point Mutation Protein Binding Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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