Open AccessThe solution structure of human endothelin‐2 a 1 H‐NMR and CD study
Author(s) -
Arvidsson Klas,
Nemoto Tadashi,
Mitsui Youji,
Ohashi Shinichi,
Nakanishi Hiroshi
Publication year - 1998
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1998.2570380.x
Subject(s) - dihedral angle , chemistry , conformational isomerism , crystallography , aqueous solution , solvent , stereochemistry , hydrogen bond , molecule , organic chemistry
The solution structure of the vasoactive endogenous 21‐amino‐acid human endothelin‐2 has been determined by NMR and CD techniques, in a mixed solvent of 100 mM aqueous acetic acid and 25 % (by vol.) 1,1,1,3,3,3‐hexafluoro‐2‐propanol. From NMR‐derived restraints on upper limit distances and dihedral angles, distance geometry structures were calculated using the program DADAS90, and refined by simulated annealing in X‐PLOR. The structure of endothelin‐2 consists of an α‐helix of residues 9 to 17, orientated anti‐parallel to a short β‐strand of residues 1 to 3, linked together by a possible β‐turn type I of residues 5−8. These secondary structural elements are stabilised and positioned by two disulphide bonds between residues 1 and 15, and 3 and 11, respectively. The average root mean square deviation over residues 1−17 of 15 accepted low‐energy conformers chosen to reflect the solution structure of endothelin‐2, was 0.73 Å for the backbone and 1.41 Å for all heavy atoms. The data on endothelin‐2 will be discussed and compared with what has been published on other endothelin/sarafotoxin peptides.