Structural analysis and disulfide-bridge pairing of two odorant-binding proteins from Bombyx mori.
Pheromone-binding protein (PBP) and general odorant-binding proteins (GOBPs) were purified from the antennae of Bombyx mori and structurally characterised. The amino acid sequence of GOBP-2 has been corrected. The disulphide arrangements of PBP and GOBP-2 have been determined by a combined mass spectrometric/Edman degradation approach. The same cysteine pairings, Cys19-Cys54, Cys50-Cys108, and Cys97-Cys117, were found in both proteins, suggesting that such patterns occur commonly throughout this family of molecules. This arrangement of disulphide bonds indicates that the three-dimensional structure of insect OBPs is defined by three loops, rich in helical content, which can vary in size and charge distribution from one protein to another.
Scaloni
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Centro Internazionale Servizi di Spettrometria di Massa-IABBAM, National Research Council, Naples, 80131, Italy. ascaloni@saul.iabbam.na.cnr.it
Monti
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Angeli
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Pelosi
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D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000737:chemistry*; D002628:Chemoreceptor Cells / Q000737:chemistry; D017124:Conserved Sequence; D004220:Disulfides / Q000737:chemistry*; D019476:Insect Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D018035:Receptors, Odorant / Q000737:chemistry*; D017385:Sequence Homology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D004220:Disulfides; D019476:Insect Proteins; D010446:Peptide Fragments; D018035:Receptors, Odorant; C045648:odorant-binding protein