P. Luginbuhl et al., THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-11 FROM THE CILIATED PROTOZOAN EUPLOTES-RAIKOVI, Protein science, 5(8), 1996, pp. 1512-1522
The NMR solution structure of the pheromone Er-11, a 39-residue protei
n from the ciliated protozoan Euplotes raikovi, was calculated with th
e distance geometry program DIANA from 449 NOE upper distance constrai
nts and 97 dihedral angle constraints, and the program OPAL was employ
ed for structure refinement by molecular mechanics energy minimization
in a water bath. For a group of 20 conformers used to characterize th
e solution structure, the average of the pairwise RMS deviations from
the mean structure calculated for the backbone heavy atoms N, C-alpha,
and C' of residues 2-38 was 0.30 Angstrom. The molecular architecture
is dominated by an up-down-up bundle of three short helices with resi
dues 2-9, 12-19, and 22-32, which is closely similar to the previously
determined structures of the homologous pheromones Er-1, Er-2, and Er
-10. This finding provides structural evidence for the capability show
n by these pheromones to compete with each other in binding reactions
to their cell-surface receptors.