Solution conformation of endothelin determined by means of 1H-NMR spectroscopy and distance geometry calculations.
The structure of endothelin-1 (ET-1), an endothelial cell-derived peptide with vasoconstricting activity, was determined in an aqueous solution by means of a combination of NMR and distance geometry calculations. The resulting structure is characterized by an alpha-helical conformation in the sequence region, Lys9-Cys15. Furthermore, an extended structure and a turn structure exist in the Cys1-Ser4 and Ser5-Asp8 regions respectively, and no preferred conformation was found for the C-terminal part of the peptide which was not uniquely constrained by the NMR data. These structural elements, the alpha-helical structure in the sequence portion, Cys-X-X-X-Cys, and the extended structure in Cys-X-Cys, are homologous to those found commonly in several neurotoxic peptides.
Tamaoki
H
H
Institute for Protein Research, Osaka University, Japan.
Kobayashi
Y
Y
Nishimura
S
S
Ohkubo
T
T
Kyogoku
Y
Y
Nakajima
K
K
Kumagaye
S
S
Kimura
T
T
Sakakibara
S
S
D000465:Algorithms; D000595:Amino Acid Sequence; D016232:Endothelins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D012996:Solutions; D013329:Structure-Activity Relationship
D016232:Endothelins; D012996:Solutions