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The crystal structure of human endothelin

Nature Structural Biology volume 1, pages 311–319 (1994)Cite this article

Abstract

The three–dimensional structure of the vasoactive polypeptide endothelin, the most potent vasocontrictor yet identified, has been determined by X–ray crystallography to 2.18 Å resolution. This intermediate–sized structure was solved by molecular replacement techniques using a fragment of an NMR–derived model for initial phasing of the data. However, comparisons of the final X–ray structure with the many diverse models derived from NMR data indicate some important differences, especially in the carboxy–terminal region of the molecule: the entire carboxy terminal tail (residues 16–21) is helical in the crystal structure, but not in any of the NMR structures. This may be a functionally significant difference as this region is crucial for receptor binding and vasoactivity.

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  1. Diane H. Peapus

    Present address: Department of Chemistry, Rensselaer Polytechnic Institute, Troy, New York, 12180, USA

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  1. Department of Crystallography, Birkbeck College, University of London, London, WC1E 7HX, UK

    Robert W. Janes & B.A. Wallace

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Janes, R., Peapus, D. & Wallace, B. The crystal structure of human endothelin. Nat Struct Mol Biol 1, 311–319 (1994). https://doi.org/10.1038/nsb0594-311

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