Structural analysis and disulfide-bridge pairing of tow odorant-binding proteins from Bombyx mori
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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.