Journal article
Cross-Chimeric Analysis of Selectivity of Secretin and VPAC1 Receptor Activation 1 1 This work was supported by grants from the National Institutes of Health (DK46577) and the Fiterman Foundation. 2 2 These authors contributed equally to this work.
Abstract
Agonist action at receptors is highly specific, affected by the structure of both ligand and receptor. Chimeric constructs of structurally related receptors and/or ligands that have biological differences provide an opportunity to correlate a specific structural domain with function. In this work, we have used a cross-chimeric approach to explore the structural basis for rat secretin and vasoactive intestinal polypeptide action at their closely …
Authors
Park C-G; Ganguli SC; Pinon DI; Hadac EM; Miller LJ
Journal
Journal of Pharmacology and Experimental Therapeutics, Vol. 295, No. 2, pp. 682–688
Publisher
Elsevier
Publication Date
November 2000
DOI
10.1016/s0022-3565(24)38956-6
ISSN
0022-3565
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceAnimalsBinding SitesCHO CellsCOS CellsCricetinaeLigandsMolecular Sequence DataProtein FoldingProtein Structure, TertiaryReceptors, G-Protein-CoupledReceptors, Gastrointestinal HormoneReceptors, Vasoactive Intestinal PeptideReceptors, Vasoactive Intestinal Polypeptide, Type IRecombinant Fusion ProteinsSecretinSequence Homology, Amino AcidStructure-Activity RelationshipSubstrate SpecificityVasoactive Intestinal Peptide