Biochem Biophys Res Commun. 1991 Jul 31;178(2):570-7.

The conformation of endothelin-1 in aqueous solution: NMR-derived constraints combined with distance geometry and molecular dynamics calculations.

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Parke-Davis Pharmaceutical Research Division, Warner Lambert Company, Ann Arbor, MI 48105.

Abstract

The aqueous solution conformation of the bicyclic, 21 amino acid vasoconstrictor peptide, endothelin-1, has been determined using two dimensional NMR and a combination of distance geometry and molecular dynamics. The dominant structural feature is a helical region between Lys9 and Cys15 characterized by strong NHi-NHi+1 NOEs and several long range NOEs spanning 3 to 5 residues. Solvent inaccessibility and possible hydrogen bonding in the Cys3-Cys11 loop is suggested by the temperature independence of the chemical shifts of several amide protons. There is no evidence for association of the C-terminal hexapeptide with the bicyclic region.

PMID:: 1859417; [PubMed - indexed for MEDLINE]

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Endothelins

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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. [FEBS Lett. 1991]
Solution conformation of endothelin, a potent vaso-constricting bicyclic peptide. A combined use of 1H NMR spectroscopy and distance geometry calculations.
Munro S, Craik D, McConville C, Hall J, Searle M, Bicknell W, Scanlon D, Chandler C. FEBS Lett. 1991 Jan 14; 278(1):9-13.
Solution conformation of endothelin-1 by 1H NMR, CD, and molecular modeling. [Int J Pept Protein Res. 1991]
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Saudek V, Hoflack J, Pelton JT. Int J Pept Protein Res. 1991 Mar; 37(3):174-9.
Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry. [FEBS Lett. 1989]
Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry.
Endo S, Inooka H, Ishibashi Y, Kitada C, Mizuta E, Fujino M. FEBS Lett. 1989 Oct 23; 257(1):149-54.
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Review [Multi-dimensional NMR and its application to the structural analysis of proteins]. [Tanpakushitsu Kakusan Koso. 1992]
Review [Multi-dimensional NMR and its application to the structural analysis of proteins].
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Cited by 2 PubMed Central articles

Modeling and docking the endothelin G-protein-coupled receptor. [Biophys J. 2000]
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Orry AJ, Wallace BA. Biophys J. 2000 Dec; 79(6):3083-94.
A comparison of X-ray and NMR structures for human endothelin-1. [Protein Sci. 1995]
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Biochem Biophys Res Commun. 1991 Jul 31 ;178(2):570-7.

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