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...

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Bibliographic Details
Published inInternational journal of peptide and protein research Vol. 36; no. 2; p. 128
Main Authors Perkins, T D, Hider, R C, Barlow, D J
Format Journal Article
LanguageEnglish
Published Denmark 01.08.1990
Subjects
Amino Acid Sequence
Animals
Circular Dichroism
Endothelins - chemistry
Mammals
Models, Chemical
Molecular Sequence Data
Protein Conformation
Solutions
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Summary: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.
ISSN:0367-8377
DOI:10.1111/j.1399-3011.1990.tb00955.x