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Structure of Bombyx mori chemosensory protein 1 in solution
Author(s) -
Jansen Séverine,
Chmelík Josef,
Žídek Lukáš,
Padrta Petr,
Novák Petr,
Zdráhal Zbyněk,
Picimbon JeanFrançois,
Löfstedt Christer,
Sklenář Vladimír
Publication year - 2007
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20205
Subject(s) - bombyx mori , biology , insect , complementary dna , bombyx , biochemistry , peptide sequence , globular protein , leucine , amino acid , botany , gene
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.