Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of Bombyx mori chemosensory protein 1 in solution.,Jansen S, Chmelik J, Zidek L, Padrta P, Novak P, Zdrahal Z, Picimbon JF, Lofstedt C, Sklenar V Arch Insect Biochem Physiol. 2007 Nov;66(3):135-45. PMID:17966128[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jansen S, Chmelik J, Zidek L, Padrta P, Novak P, Zdrahal Z, Picimbon JF, Lofstedt C, Sklenar V. Structure of Bombyx mori chemosensory protein 1 in solution. Arch Insect Biochem Physiol. 2007 Nov;66(3):135-45. PMID:17966128 doi:http://dx.doi.org/10.1002/arch.20205
