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Biochem Biophys Res Commun


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
Year:1999
Volume:266
Issue:2
Page Number:386 - 391
DOI: 10.1006/bbrc.1999.1791
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"

 
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