Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry.
The solution conformation of endothelium-derived vasoconstrictor peptide, endothelin, has been determined by two-dimensional 1H-NMR spectroscopy and distance geometry. Conformation in the N-terminal core region (residues 1-15) is well-defined and a characteristic is the helix-like conformation in the segment from Lys9 to Cys15. Contrarily, the C-terminal tail region (residues 16-21) does not assume a defined conformation and there are no specific interactions between the core and the tail regions.
Endo
S
S
Tsukuba Research Laboratories, Takeda Chemical Industries Ltd, Japan.
Inooka
H
H
Ishibashi
Y
Y
Kitada
C
C
Mizuta
E
E
Fujino
M
M
D000595:Amino Acid Sequence; D000818:Animals; D016232:Endothelins; D004730:Endothelium, Vascular; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008433:Mathematics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides; D011487:Protein Conformation; D012984:Software; D012996:Solutions
D016232:Endothelins; D010455:Peptides; D012996:Solutions; D006859:Hydrogen