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Solution conformation of endothelin, a potent vaso-constricting bicyclic peptide. A combined use of 1H NMR spectroscopy and distance geometry calculations.

作者信息

Munro S, Craik D, McConville C, Hall J, Searle M, Bicknell W, Scanlon D, Chandler C

机构信息

School of Pharmaceutical Chemistry, Victorian College of Pharmacy Ltd., Parkville, Australia.

出版信息

FEBS Lett. 1991 Jan 14;278(1):9-13. doi: 10.1016/0014-5793(91)80071-a.

DOI:10.1016/0014-5793(91)80071-a
PMID:1993480
Abstract

The solution structure of endothelin-1, a newly discovered potent bicyclic peptide vaso-constrictor agent, has been investigated using 1H NMR conformational constraints and distance geometry calculations. The conformation is constrained by two disulphide bridges between Cys1-Cys15 and Cys3-Cys11 but the NMR data and computed conformers show additional helical structure between residues Leu6 and Cys11. Our results are compared with previous conflicting reports on the solution conformation of this peptide.

摘要

相似文献

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