Soluble low molecular weight acidic proteins are suspected to transport stimulus molecules to the sensory neurons within insect sensilla. From the antennae of Bombyx mori, we have purified and sequenced a protein (BmorCSP1) bearing sequence similarity to a class of soluble chemosensory proteins rece
Structure of Bombyx mori chemosensory protein 1 in solution
✍ Scribed by Séverine Jansen; Josef Chmelík; Lukáš Žídek; Petr Padrta; Petr Novák; Zbyněk Zdráhal; Jean-François Picimbon; Christer Löfstedt; Vladimír Sklenář
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 361 KB
- Volume
- 66
- Category
- Article
- ISSN
- 0739-4462
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✦ Synopsis
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 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.
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