Séverine Jansen and Josef Chmelík both contributed equally to this work.
Structure of Bombyx mori chemosensory protein 1 in solution †
Version of Record online: 26 OCT 2007
Copyright © 2007 Wiley-Liss, Inc.
Archives of Insect Biochemistry and Physiology
Volume 66, Issue 3, pages 135–145, November 2007
How to Cite
Jansen, S., Chmelík, J., Žídek, L., Padrta, P., Novák, P., Zdráhal, Z., Picimbon, J.-F., Löfstedt, C. and Sklenář, V. (2007), Structure of Bombyx mori chemosensory protein 1 in solution . Arch. Insect Biochem. Physiol., 66: 135–145. doi: 10.1002/arch.20205
- Issue online: 26 OCT 2007
- Version of Record online: 26 OCT 2007
- Manuscript Accepted: 30 APR 2007
- Manuscript Received: 20 FEB 2007
- Ministry of Education, Youth, and Physical Culture of the Czech Republic. Grant Numbers: MSM0021622413, MSM0221622415, LC06030
- Grant Agency of the Czech Republic. Grant Number: 204/03/H016
- Swedish Research Council (VR)
- Crafoord Foundation
- Research School of Functional Genomics and Bioinformatics (Göteborg)
- Bombyx mori;
- chemosensory proteins;
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 mori 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 α-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. Arch. Insect Biochem. Physiol. 66:135–145, 2007. © 2007 Wiley-Liss, Inc.