Proposed solution structure of endothelin.
A model is proposed for the 3-dimensional structure of endothelin, a potent vasoconstrictor and pressor peptide from vascular endothelium. The model is derived through protein structure prediction and circular dichroism studies, and is based on the atomic coordinates for the bee-venom peptide apamin. The model derived shows the same turn-helix motif as observed for apamin and mast-cell degranulating peptide. On the basis of this model we suggest possible strategies for endothelin antagonist design, and note that this motif may be common in a number of peptides acting on channel proteins.
Perkins
T D
TD
Department of Pharmacy, King's College, London, England.
Hider
R C
RC
Barlow
D J
DJ
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D016232:Endothelins / Q000737:chemistry*; D008322:Mammals; D008956:Models, Chemical; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012996:Solutions
D016232:Endothelins; D012996:Solutions