Pheromone binding structure

Timm, D. E., Baker, L. J., Mueller, H., Zidek, L. and Novotny, M. V. (2001) Structural basis of pheromone binding to mouse major urinary protein (MUP-I). Protein Sci. 10, 997-1004. 

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. 

Sandler B. H., Nikonova L., Leal W. S. and Clardy J. (2000) Sexual attraction in the silkworm moth structure of the pheromone-binding-protein-bombykol complex. Chem. Biol. 7, 143-151. 

Du G. and Prestwich G. D. (1995) Protein structure encodes the ligand binding specificity in pheromone binding proteins. Biochemistry 34, 8726-8732. 

Leal W. S., Nikonova L. and Peng G. (1999) Disulfide structure of the pheromone binding protein from the silkworm moth, Bombyx mori. FEBS Letters. 468, 85-90. 

Raming K., Krieger J. and Breer H. (1990) Primary structure of a pheromone-binding protein from Antheraea pernyi homologies with other ligand-carrying proteins. J. Comp. Physiol. B 160, 503-509. 

Between pH 5.5 and 6.5, there is a dramatic increase in binding, suggesting that an amino acid with a pKa 6.0 has a strong effect on pheromone binding. Because this ionization is seen for all PBPs studied so far, the most likely candidate for this effect is one (or more) of the conserved histidine residues. Recently, the structure of the acid form of B. mori PBP was solved (Horst et al.,... 

Horst R., Damberger F., Luginbuehl P., Guentert P., Peng G., Nikanova L., Leal W. S. and Wuethrich K. (2001) NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. Proc. Natl. Acad. Sci. 98, 14374—14379. 

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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