Structure of Bombyx mori chemosensory protein 1 in solution

Severine Jansen; Josef Chmelik; Lukas Zidek; Petr Padrta; Petr Novak; Zbynek Zdrahal; Jean-Francois Picimbon; Christer Löfstedt; Vladimir Sklenar

doi:10.1002/arch.20205

Structure of Bombyx mori chemosensory protein 1 in solution

Severine Jansen, Josef Chmelik, Lukas Zidek, Petr Padrta, Petr Novak, Zbynek Zdrahal, Jean-Francois Picimbon, Christer Löfstedt, Vladimir Sklenar

Forskningsoutput: Tidskriftsbidrag › Artikel i vetenskaplig tidskrift › Peer review

Sammanfattning

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 morii 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 a-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.

Originalspråk	engelska
Sidor (från-till)	135-145
Tidskrift	Archives of Insect Biochemistry and Physiology
Volym	66
Nummer	3
DOI	https://doi.org/10.1002/arch.20205
Status	Published - 2007

Ämnesklassifikation (UKÄ)

Zoologi
Biologi

Tillgång till dokument

10.1002/arch.20205

Evolutionära mekanismer hos feromondivergenser inom Lepidoptera
Löfstedt, C. (PI), Wang, H.-L. (Forskare), Ding, B. (Forskare), Zhang, D.-D. (Forskare), Svensson, G. (PI), Andersson, M. N. (Forskare), Jirle, E. (Forskare), Xia, Y. (Forskarstuderande), Hou, X. (Forskarstuderande), Yuvaraj, J. K. (Forskare) & Tóth, E. (Forskare)
1995/01/01 → 2019/12/31
Projekt: Forskning

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@article{d537f58ed3b74c85ba7303a5fe642ed6,

title = "Structure of Bombyx mori chemosensory protein 1 in solution",

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 morii 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 a-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.",

keywords = "Bombyx mori, chemosensory proteins, NMR",

author = "Severine Jansen and Josef Chmelik and Lukas Zidek and Petr Padrta and Petr Novak and Zbynek Zdrahal and Jean-Francois Picimbon and Christer L{\"o}fstedt and Vladimir Sklenar",

year = "2007",

doi = "10.1002/arch.20205",

language = "English",

volume = "66",

pages = "135--145",

journal = "Archives of Insect Biochemistry and Physiology",

issn = "1520-6327",

publisher = "John Wiley & Sons Inc.",

number = "3",

}

TY - JOUR

T1 - Structure of Bombyx mori chemosensory protein 1 in solution

AU - Jansen, Severine

AU - Chmelik, Josef

AU - Zidek, Lukas

AU - Padrta, Petr

AU - Novak, Petr

AU - Zdrahal, Zbynek

AU - Picimbon, Jean-Francois

AU - Löfstedt, Christer

AU - Sklenar, Vladimir

PY - 2007

Y1 - 2007

N2 - 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 morii 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 a-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.

AB - 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 morii 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 a-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.

KW - Bombyx mori

KW - chemosensory proteins

KW - NMR

U2 - 10.1002/arch.20205

DO - 10.1002/arch.20205

M3 - Article

C2 - 17966128

SN - 1520-6327

VL - 66

SP - 135

EP - 145

JO - Archives of Insect Biochemistry and Physiology

JF - Archives of Insect Biochemistry and Physiology

IS - 3

ER -

Structure of Bombyx mori chemosensory protein 1 in solution

Sammanfattning

Ämnesklassifikation (UKÄ)

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Projekt

Evolutionära mekanismer hos feromondivergenser inom Lepidoptera

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