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The NMR solution structure of the pheromone Er‐11 from the ciliated protozoan Euplotes raikovi
Author(s) -
Luginbühl Peter,
Wu Jihui,
Zerbe Oliver,
Ortenzi Claudio,
Luporini Pierangelo,
Wüthrich Kurt
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560050807
Subject(s) - dihedral angle , pheromone , conformational isomerism , crystallography , chemistry , sex pheromone , stereochemistry , residue (chemistry) , molecule , energy minimization , computational chemistry , biology , biochemistry , zoology , hydrogen bond , organic chemistry , genetics
The NMR solution structure of the pheromone E r ‐11, a 39‐residue protein from the ciliated protozoan Euplotes raikovi , was calculated with the distance geometry program DIANA from 449 NOE upper distance constraints and 97 dihedral angle constraints, and the program OPAL was employed for structure refinement by molecular mechanics energy minimization in a water bath. For a group of 20 conformers used to characterize the solution structure, the average of the pairwise RMS deviations from the mean structure calculated for the backbone heavy atoms N, C α , and C of residues 2–38 was 0.30 Å. The molecular architecture is dominated by an up‐down‐up bundle of three short helices with residues 2–9, 12–19, and 22–32, which is closely similar to the previously determined structures of the homologous pheromones EM, Er‐2, and EMO. This finding provides structural evidence for the capability shown by these pheromones to compete with each other in binding reactions to their cell‐surface receptors.