Odorant binding protein

BmorPBP structure and function

This protein was first identified in the B. mori male antennae by Krieger et al. in 1996 ^[4] . It has 164 amino acids that forms 6-7 alpha helices. Three 3 disulfide bonds formed by 6 cystein residues tied four helices. As expected from a soluble protein, its surface is covered with charged residues.

BmorPBP ligand and ligand binding

The protein natural ligand is the moth pheromone bombykol. However, it was demonstrated that other molecules can also bound to the protein cavity ^[5]. The interaction with the ligand is beeing made by 4 alpha helices in the core of the protein, which form the binding cavity ^[6].

Protein conformations

The PBP has two pH-dependent conformations, with different ligand affinities: the "open form" (A) and the "close form" (B) ^[7]. The pheromone bombykol, and the seventh α-helix loacated in the C terminus of the protein compete for the binding site. In a nuetral pH (6.5-7) the protein is in the "open form" (A), in which the

The C terminus of the protein bears mostly nonpolar amino acids. Yet on the surface of the helix there are three exceptional amino acids: Asp-132, Glu-137, and Glu-141, which are conserved in moth PBP ^[8].

. Of these, residues Asp-132 and Glu-141 form a molecular switch, which upon protonation at low pH triggers the formation of the C-terminal α-helix (101).

• "open form" (A)
• "close form" (B)

• The pH dependent theory

According to this theory,

Receptor activation

The surface of the dendrite is negatively charged ^[9], which cause the accumulation of positively charged kations near the membrane surface (20-50 nm), thereby inducing a low pH environment near the dendrite membrane kaissling 2009

Leal WS, et al. (2005) Kinetics and molecular properties of pheromone binding and release. Proc Natl Acad Sci USA 102(15):5386–5391.

• The other theory

The BPB ligand is the moth pheromone