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Structure of Bombyx mori chemosensory protein 1 in solution

På svenska

Author

  • Severine Jansen
  • Josef Chmelik
  • Lukas Zidek
  • Petr Padrta
  • Petr Novak
  • Zbynek Zdrahal
  • Jean-Francois Picimbon
  • Christer Löfstedt
  • Vladimir Sklenar

Summary, in English

Chemosensory Proteins (CSPs) represent a family of conserved proteins found in insects that may be involved in chemosensory functions. BmorCSP1 is expressed mainly in antennae and legs of the silkworm moth Bombyx morii and was cloned from antennal cDNA. Here we report the determination of the structure of Bombyx mori CSP1 (BmorCSP1) by NMR. The overall fold of BmorCSP1 is globular and comprises six a-helices. These helices span residues 10-14, 17-27, 35-49, 57-72, 75-85, and 92-100. The internal hydrophobic sides of the helices are formed mostly by leucine and isoleucine residues and, therefore, well suited to constitute a binding site for hydrophobic ligands.

Publishing year

2007

Language

English

Pages

135-145

Publication/Series

Archives of Insect Biochemistry and Physiology

Volume

66

Issue

3

Document type

Journal article

Publisher

John Wiley & Sons Inc.

Topic

  • Zoology
  • Biological Sciences

Keywords

  • Bombyx mori
  • chemosensory proteins
  • NMR

Status

Published

Project

  • Evolutionary mechanisms of pheromone divergence in Lepidoptera

Research group

  • Pheromone Group

ISBN/ISSN/Other

  • ISSN: 1520-6327