Proposed solution structure of endothelin

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Abstract
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.