2JNT
Structure of Bombyx mori Chemosensory Protein 1 in Solution
Summary for 2JNT
| Entry DOI | 10.2210/pdb2jnt/pdb |
| NMR Information | BMRB: 6943 |
| Descriptor | Chemosensory protein CSP1 (1 entity in total) |
| Functional Keywords | bmorcsp1, csp1, ligand binding protein |
| Biological source | Bombyx mori (domestic silkworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 12558.27 |
| Authors | Jansen, S.,Zidek, L.,Chmelik, J.,Novak, P.,Padrta, P.,Picimbon, J.,Lofstedt, C.,Sklenar, V. (deposition date: 2007-02-02, release date: 2007-11-20, Last modification date: 2024-11-06) |
| Primary citation | Jansen, S.,Chmelik, J.,Zidek, L.,Padrta, P.,Novak, P.,Zdrahal, Z.,Picimbon, J.-F.,Lofstedt, C.,Sklenar, V. Structure of Bombyx mori chemosensory protein 1 in solution Arch.Insect Biochem.Physiol., 66:135-145, 2007 Cited by PubMed 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 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. PubMed: 17966128DOI: 10.1002/arch.20205 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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