Structure of Bombyx mori chemosensory protein 1 in solution

JANSEN, Séverine, Josef CHMELÍK, Lukáš ŽÍDEK, Petr PADRTA, Petr NOVÁK, Zbyněk ZDRÁHAL, Jean-François PICIMBON, Christer LÖFSTEDT and Vladimír SKLENÁŘ. Structure of Bombyx mori chemosensory protein 1 in solution. Archives of Insect Biochemistry and Physiology. Wiley, 2007, vol. 66, No 3, p. 135-145. ISSN 0739-4462.

Basic information

• Original name: Structure of Bombyx mori chemosensory protein 1 in solution
• Name in Czech: Structure of Bombyx mori chemosensory protein 1 in solution
• Authors: JANSEN, Séverine (250 France), Josef CHMELÍK (203 Czech Republic), Lukáš ŽÍDEK (203 Czech Republic, guarantor), Petr PADRTA (203 Czech Republic), Petr NOVÁK (203 Czech Republic), Zbyněk ZDRÁHAL (203 Czech Republic), Jean-François PICIMBON (250 France), Christer LÖFSTEDT (752 Sweden) and Vladimír SKLENÁŘ (203 Czech Republic).
• Edition: Archives of Insect Biochemistry and Physiology, Wiley, 2007, 0739-4462.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 1.345
• RIV identification code: RIV/00216224:14310/07:00020544
• Organization unit: Faculty of Science
• UT WoS: 000250321200003
• Keywords in English: Bombyx mori; Chemosensory proteins; NMR
• Tags: Bombyx mori, Chemosensory proteins, NMR
• Tags: International impact, Reviewed

Abstract

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.

Abstract (in Czech)

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.

Links

• GD204/03/H016, research and development project: Name: Strukturní biofyzika makromolekul

Investor: Czech Science Foundation, Structural biophysics of macromolecules

• LC06030, research and development project: Name: Biomolekulární centrum

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre

• MSM0021622413, plan (intention): Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

• MSM0021622415, plan (intention): Name: Molekulární podstata buněčných a tkáňových regulací

Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations