| Title: | Structural analysis and disulfide-bridge pairing of two odorant-binding proteins from Bombyx mori |
| Author(s): | Scaloni A; Monti M; Angeli S; Pelosi P; |
| Address: | "Centro Internazionale Servizi di Spettrometria di Massa-IABBAM, National Research Council, Naples, 80131, Italy. ascaloni@saul.iabbam.na.cnr.it" |
| Journal Title: | Biochem Biophys Res Commun |
| ISSN/ISBN: | 0006-291X (Print) 0006-291X (Linking) |
| Abstract: | "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" |
| Keywords: | "Amino Acid Sequence Animals Bombyx/*chemistry Chemoreceptor Cells/chemistry Conserved Sequence Disulfides/*chemistry Insect Proteins/chemistry Molecular Sequence Data Peptide Fragments/analysis Protein Binding Receptors, Odorant/*chemistry Sequence Homolo;" |
| Notes: | "MedlineScaloni, A Monti, M Angeli, S Pelosi, P eng Research Support, Non-U.S. Gov't 1999/12/22 Biochem Biophys Res Commun. 1999 Dec 20; 266(2):386-91. doi: 10.1006/bbrc.1999.1791" |
