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The NMR solution structure of the pheromone er-11 from the ciliated protozoan euplotes raikovi

Academic Article
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Overview

authors

  • Luginbuhl, P.
  • Wu, J. H.
  • Zerbe, O.
  • Ortenzi, C.
  • Luporini, P.
  • Wuthrich, Kurt

publication date

  • August 1996

journal

  • Protein Science  Journal

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.

subject areas

  • Amino Acid Sequence
  • Animals
  • Carbon Isotopes
  • Euplotes
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Pheromones
  • Protein Structure, Tertiary
  • Protozoan Proteins
  • Stereoisomerism
  • Tritium
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Research

keywords

  • NMR structure
  • cellular recognition
  • pheromone Er-11 from Euplotes raikovi
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Identity

PubMed Central ID

  • PMC2143477

International Standard Serial Number (ISSN)

  • 0961-8368

Digital Object Identifier (DOI)

  • 10.1002/pro.5560050807

PubMed ID

  • 8844842
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Additional Document Info

start page

  • 1512

end page

  • 1522

volume

  • 5

issue

  • 8

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