Conformation of endothelin in aqueous ethylene glycol determined by 1H‐NMR and molecular dynamics simulations

FEBS Letters

Krystek, Stanley R.¹ 

[1]Department of Macromolecular Modeling, Bristol-Myers Squibb Research Institute, Princeton, NJ 08543-4000, USA

关键词: Endothelin;    NMR;    Molecular dynamics;    Three dimensional structure;   

DOI  :  10.1016/0014-5793(91)80396-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The solution conformation of a 21-residue vasoconstrictor peptide endothelin-1 (ET-1) in water-ethylene glycol has been determined by two-dimensional ¹H-NMR spectroscopy and constrained molecular dynamics simulations. The N-terminus (residues 1–4) appears to undergo conformational averaging and no single structure consistent with the NMR constraints could be found for this region. Residues 5–8 form a turn, and residues 9–16 exist in a helical conformation. A flexible ‘hinge’ between residues 8–9 allows various orientations of the turn relative to the helix. Another ‘hinge’ at residue 17 connects the extended C-terminus to the bicyclic core region (residues 1–15). Residues important for binding and biological activity form a contiguous surface on one side of the helix, with the two disulfides extending from the other side of the helix.

【 授权许可】

Unknown