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Structure of Bombyx mori chemosensory protein 1 in solution

Jansen, Severine LU ; Chmelik, Josef; Zidek, Lukas; Padrta, Petr; Novak, Petr; Zdrahal, Zbynek; Picimbon, Jean-Francois LU ; Löfstedt, Christer LU and Sklenar, Vladimir (2007) In Archives of Insect Biochemistry and Physiology 66(3). p.135-145
Abstract
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.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Bombyx mori, chemosensory proteins, NMR
in
Archives of Insect Biochemistry and Physiology
volume
66
issue
3
pages
135 - 145
publisher
John Wiley & Sons
external identifiers
  • wos:000250321200003
  • scopus:36749012340
ISSN
1520-6327
DOI
10.1002/arch.20205
project
Evolutionary mechanisms of pheromone divergence in Lepidoptera
language
English
LU publication?
yes
id
d537f58e-d3b7-4c85-ba73-03a5fe642ed6 (old id 654198)
date added to LUP
2007-12-13 10:21:10
date last changed
2017-09-17 05:04:37
@article{d537f58e-d3b7-4c85-ba73-03a5fe642ed6,
  abstract     = {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 <i>Bombyx mori</i>i 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.},
  author       = {Jansen, Severine and Chmelik, Josef and Zidek, Lukas and Padrta, Petr and Novak, Petr and Zdrahal, Zbynek and Picimbon, Jean-Francois and Löfstedt, Christer and Sklenar, Vladimir},
  issn         = {1520-6327},
  keyword      = {Bombyx mori,chemosensory proteins,NMR},
  language     = {eng},
  number       = {3},
  pages        = {135--145},
  publisher    = {John Wiley & Sons},
  series       = {Archives of Insect Biochemistry and Physiology},
  title        = {Structure of <i>Bombyx mori</i> chemosensory protein 1 in solution},
  url          = {http://dx.doi.org/10.1002/arch.20205},
  volume       = {66},
  year         = {2007},
}