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. 1992 Jun 23;31(24):5640-5.
doi: 10.1021/bi00139a030.

Solution structure of endothelin-3 determined using NMR spectroscopy

R G Mills  1 , S I O'Donoghue, R Smith, G F King
Affiliations

Solution structure of endothelin-3 determined using NMR spectroscopy

R G Mills et al. Biochemistry. .

Abstract

The aqueous solution structure of the 21-residue vasoactive peptide hormone endothelin-3 has been determined using high-resolution NMR spectroscopy. A total of 177 proton-proton distance measurements and 5 chi 1 dihedral angle constraints derived from NMR spectra were used to calculate the structure using a combination of distance geometry and dynamical simulated annealing calculations. The calculations reveal a highly ordered, compact conformation in which a helical region extending from K9 to C15 lies in close apposition with the C-terminal hexapeptide; this interaction seems to be largely driven by hydrophobic interactions. Structure-activity studies are interpreted in terms of the conformational features of the calculated endothelin-3 structure.

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