J 2007

Structure of Bombyx mori chemosensory protein 1 in solution

JANSEN, Séverine, Josef CHMELÍK, Lukáš ŽÍDEK, Petr PADRTA, Petr NOVÁK et. al.

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

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

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

Tags

International impact, Reviewed
Změněno: 26/6/2009 10:22, prof. RNDr. Zbyněk Zdráhal, Dr.

Abstract

ORIG CZ

V originále

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.

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