Proposed solution structure of endothelin.

T D Perkins; R C Hider; D J Barlow

doi:10.1111/j.1399-3011.1990.tb00955.x

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Proposed solution structure of endothelin.

T D Perkins·R C Hider·D J Barlow

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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.

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Amino Acid Sequence Animals Circular Dichroism Endothelins Mammals Models, Chemical Molecular Sequence Data Protein Conformation Solutions Journal Article Research Support, Non-U.S. Gov't

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T D Perkins, R C Hider, D J Barlow. 1990. Proposed solution structure of endothelin.. https://doi.org/10.1111/j.1399-3011.1990.tb00955.x

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