Solution conformation of endothelin determined by means of 1H-NMR spectroscopy and distance geometry calculations |
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Authors: | H Tamaoki Y Kobayashi S Nishimura T Ohkubo Y Kyogoku K Nakajima S Kumagaye T Kimura S Sakakibara |
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Affiliation: | Institute for Protein Research, Osaka University, Japan. |
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Abstract: | The structure of endothelin-1 (ET-1), an endothelial cell-derived peptide with vasoconstricting activity, was determined in an aqueous solution by means of a combination of NMR and distance geometry calculations. The resulting structure is characterized by an alpha-helical conformation in the sequence region, Lys9-Cys15. Furthermore, an extended structure and a turn structure exist in the Cys1-Ser4 and Ser5-Asp8 regions respectively, and no preferred conformation was found for the C-terminal part of the peptide which was not uniquely constrained by the NMR data. These structural elements, the alpha-helical structure in the sequence portion, Cys-X-X-X-Cys, and the extended structure in Cys-X-Cys, are homologous to those found commonly in several neurotoxic peptides. |
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