title: The structure of secretin family GPCR peptide ligands: implications for receptor pharmacology and drug development.
abstract: The secretin family G protein-coupled receptors, characterized by a large N-terminal extracellular domain and seven transmembrane helices, are drug targets in many diseases, including migraine, cardiovascular disease, diabetes, osteoporosis and inflammatory disorders. Their activating ligands are peptides with an average length of 30 amino acids. In this article we review the available structural data for these peptides and how this explains their activity. We emphasize how this information may be used to accelerate the development of new drugs against these receptors.
authors.affiliation: School of Biological Sciences, University of Auckland, New Zealand.
authors.forename: Harriet A
authors.initials: HA
authors.lastname: Watkins
authors.forename: Maggie
authors.initials: M
authors.lastname: Au
authors.forename: Debbie L
authors.initials: DL
authors.lastname: Hay
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015195:Drug Design; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry*; D012633:Secretin / Q000737:chemistry
chemical_list: D008024:Ligands; D010455:Peptides; D043562:Receptors, G-Protein-Coupled; D012633:Secretin