Structure of Bombyx mori chemosensory protein 1 in solution

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Authors	JANSEN Séverine CHMELÍK Josef ŽÍDEK Lukáš PADRTA Petr NOVÁK Petr ZDRÁHAL Zbyněk PICIMBON Jean-François LÖFSTEDT Christer SKLENÁŘ Vladimír
Year of publication	2007
Type	Article in Periodical
Magazine / Source	Archives of Insect Biochemistry and Physiology
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	Bombyx mori; Chemosensory proteins; NMR
Description	Chemosensory Proteins (CSPs) represent a family of conserved proteins found in insects that may be implied 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 alpha-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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