 Crystal structure of the GLP-1 receptor bound to a peptide agonistAli Jazayeri,
Mathieu Rappas,
Alastair J. H. Brown,
James Kean,
James C. Errey,
Nathan J. Robertson,
Cédric Fiez-Vandal,
Stephen P. Andrews,
Miles Congreve,
Andrea Bortolato,
Jonathan S. Mason,
Asma H. Baig,
Iryna Teobald,
Andrew S. Doré,
Malcolm Weir,
Robert M. Cooke and
Fiona H. Marshall ()
Nature, 2017, vol. 546, issue 7657, 254-258 Abstract: Abstract Glucagon-like peptide 1 (GLP-1) regulates glucose homeostasis through the control of insulin release from the pancreas. GLP-1 peptide agonists are efficacious drugs for the treatment of diabetes. To gain insight into the molecular mechanism of action of GLP-1 peptides, here we report the crystal structure of the full-length GLP-1 receptor bound to a truncated peptide agonist. The peptide agonist retains an α-helical conformation as it sits deep within the receptor-binding pocket. The arrangement of the transmembrane helices reveals hallmarks of an active conformation similar to that observed in class A receptors. Guided by this structural information, we design peptide agonists with potent in vivo activity in a mouse model of diabetes. Date: 2017 Downloads: (external link) Related works: Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:546:y:2017:i:7657:d:10.1038_nature22800 Ordering information: This journal article can be ordered from DOI: 10.1038/nature22800 Access Statistics for this article Nature is currently edited by Magdalena Skipper More articles in Nature from Nature |
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