Conformation of peptides of the secretin-VIP-glucagon family in solution.
The significance of a well defined molecular architecture in hormone receptor interaction and the methods available for the study of preferred conformations are discussed. The conformational freedom in glucagon is a major obstacle in the determination of its biologically relevant geometry. In the secretin molecule intramolecular forces generate a folded, partially helical conformation. In respect of long range cooperative interactions resulting in a compact molecule with secondary-tertiary structure secretin is similar to globular proteins. In VIP some characteristics of secretin and also of glucagon can be recognized. Further progress in conformation analysis can be expected from the study of rigid, cyclic analogs in which the biological activities of the parent hormones are retained or even enhanced. Such analogs have well defined conformations without external stabilization from membrane mimicking lipids. Therefore, they provide information on the biologically relevant geometry of the hormones and contribute also to our knowledge of receptor sites.
D000595:Amino Acid Sequence; D001665:Binding Sites; D005934:Glucagon / Q000031:analogs & derivatives; D010456:Peptides, Cyclic / Q000138:chemical synthesis; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism; D012633:Secretin / Q000031:analogs & derivatives; D014660:Vasoactive Intestinal Peptide / Q000031:analogs & derivatives
D010456:Peptides, Cyclic; D011956:Receptors, Cell Surface; D012633:Secretin; D014660:Vasoactive Intestinal Peptide; D005934:Glucagon