title: The conformation of endothelin-1 in aqueous solution: NMR-derived constraints combined with distance geometry and molecular dynamics calculations.
abstract: The aqueous solution conformation of the bicyclic, 21 amino acid vasoconstrictor peptide, endothelin-1, has been determined using two dimensional NMR and a combination of distance geometry and molecular dynamics. The dominant structural feature is a helical region between Lys9 and Cys15 characterized by strong NHi-NHi+1 NOEs and several long range NOEs spanning 3 to 5 residues. Solvent inaccessibility and possible hydrogen bonding in the Cys3-Cys11 loop is suggested by the temperature independence of the chemical shifts of several amide protons. There is no evidence for association of the C-terminal hexapeptide with the bicyclic region.
authors.affiliation: Parke-Davis Pharmaceutical Research Division, Warner Lambert Company, Ann Arbor, MI 48105.
authors.forename: M D
authors.initials: MD
authors.lastname: Reily
authors.forename: J B
authors.initials: JB
authors.lastname: Dunbar
mesh_terms: D000595:Amino Acid Sequence; D016232:Endothelins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008433:Mathematics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D016232:Endothelins