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Structure of Bombyx mori chemosensory protein 1 in solution

  • Severine Jansen
  • Josef Chmelik
  • Lukas Zidek
  • Petr Padrta
  • Petr Novak
  • Zbynek Zdrahal
  • Jean-Francois Picimbon
  • Christer Löfstedt
  • Vladimir Sklenar
Publiceringsår: 2007
Språk: Engelska
Sidor: 135-145
Publikation/Tidskrift/Serie: Archives of Insect Biochemistry and Physiology
Volym: 66
Nummer: 3
Dokumenttyp: Artikel i tidskrift
Förlag: John Wiley & Sons


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.


  • Zoology
  • Biological Sciences
  • Bombyx mori
  • chemosensory proteins
  • NMR


  • Evolutionary mechanisms of pheromone divergence in Lepidoptera
  • Pheromone Group
  • ISSN: 1520-6327

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