Structure of Bombyx mori chemosensory protein 1 in solution
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/654198
- author
- Jansen, Severine LU ; Chmelik, Josef ; Zidek, Lukas ; Padrta, Petr ; Novak, Petr ; Zdrahal, Zbynek ; Picimbon, Jean-Francois LU ; Löfstedt, Christer LU and Sklenar, Vladimir
- organization
- publishing date
- 2007
- 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 Inc.
- external identifiers
-
- wos:000250321200003
- scopus:36749012340
- pmid:17966128
- 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
- 2016-04-01 12:15:19
- date last changed
- 2024-05-07 10:40:32
@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}}, keywords = {{Bombyx mori; chemosensory proteins; NMR}}, language = {{eng}}, number = {{3}}, pages = {{135--145}}, publisher = {{John Wiley & Sons Inc.}}, 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}}, doi = {{10.1002/arch.20205}}, volume = {{66}}, year = {{2007}}, }