Pheromone binding protein structure

Fig. 2.6 Structures of the pheromone binding protein (form A) from the silk moth Bombyx mori [96] obtained in six iterative cycles of combined...

Insect OBPs are secretory proteins whose only posttranslational modification is the formation of three disulfide bridges [39,45] from six cysteine residues. That six cysteine residues are well conserved in OBPs from species of the same order is a hallmark of these proteins. The disulfide links of OBPs in a few species have been determined by analytical methods, first in the OBPs from B. mori [45,46]. As part of our attempt to get better insight into the structural biology of pheromone-binding proteins, we have determined the disulfide linkages... 

Recently, the structure of a pheromone-binding protein from the cockroach Leucophaea maderae, LmadPBP (Fig. 8b) has been solved by X-ray crystallography [58]. Despite the fact that LmadPBP and BmorPBP shared low amino acid identity (15% similarity 22%) (Fig. 9), the two proteins present similar folds. 

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Campanacci V., Longhi S., Nagnan-Le Meillour P., Cambillau C. and Tegoni, M. (1999) Recombinant pheromone binding protein 1 from Mamestra brassicae (MbraPBPl). Functional and structural characterization. Eur. J. Biochem. 264, 707-716. 

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