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The NMR solution structure of the pheromone Er-11 from the ciliated protozoan Euplotes raikovi.

Authors
  • Luginbühl, P
  • Wu, J
  • Zerbe, O
  • Ortenzi, C
  • Luporini, P
  • Wüthrich, K
Type
Published Article
Journal
Protein science : a publication of the Protein Society
Publication Date
Aug 01, 1996
Volume
5
Issue
8
Pages
1512–1522
Identifiers
PMID: 8844842
Source
Medline
License
Unknown

Abstract

The NMR solution structure of the pheromone Er-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 alpha, and C' of residues 2-38 was 0.30 A. 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 Er-1, Er-2, and Er-10. 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.

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