Solution structure of endothelin-3 determined using NMR spectroscopy.
The aqueous solution structure of the 21-residue vasoactive peptide hormone endothelin-3 has been determined using high-resolution NMR spectroscopy. A total of 177 proton-proton distance measurements and 5 chi 1 dihedral angle constraints derived from NMR spectra were used to calculate the structure using a combination of distance geometry and dynamical simulated annealing calculations. The calculations reveal a highly ordered, compact conformation in which a helical region extending from K9 to C15 lies in close apposition with the C-terminal hexapeptide; this interaction seems to be largely driven by hydrophobic interactions. Structure-activity studies are interpreted in terms of the conformational features of the calculated endothelin-3 structure.
Mills
R G
RG
Department of Biochemistry, University of Sydney, NSW, Australia.
O'Donoghue
S I
SI
Smith
R
R
King
G F
GF
D000595:Amino Acid Sequence; D016232:Endothelins; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012996:Solutions
D016232:Endothelins; D012996:Solutions