Pheromone binding proteins (PBP) are type of Odorant binding proteins (OBP) - soluble proteins mediating the early stages of volatiles detection in both insects and vertebrates
[1].
The volatiles (pheromones and other small hydrophobic molecules) are solubilized by the OBPs and activate the chemoreceptors.
As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee, ASP1.
Pheromone-binding protein ASP1
Chemical communication is crucial in social insects, where a complicated and delicate system of signals must be maintained in order to preserve the fragile equilibrium between the queen and the workers.
In the hive of the honey bee Apis mellifera this equilibrium exists partially due to the extraction of blend of substances called queen mandibular pheromone (QMP), by the queen [2]. The three major component of the QMP blend are: 9-keto-2(E)-decenoic acid (9-ODA) and 9-hydroxy-2(E)-decenoic acid (9-HDA R-(−) or S-(+)).
Pheromone-binding protein ASP of the honeybee Apis mellifera L. (Hymenoptera: Apidea) was first isolated and characterized by Danty et al. (1998)[3] from the bee antennae.
Pheromone-binding protein ASP of the honeybee Apis mellifera L. (Hymenoptera: Apidea) was first isolated and characterized by Danty et al. (1998)[4] from the bee antennae.
Structure
The protein is composed of 144 amino acids, which forms 6 alpha helices. Three tied four helices: disulfide 20–51 between H1 and H3, 47– 98 between H3 and H6, and 107–89 between H6 and H5.
Interaction with the ligand 9-ODA
The carboxyl end of the component 9-ODA points towards the solvent, and has no any interaction with residues of the protein. The residues in the binding site are
, and the connection between 9-ODA and ASP1 involve hydrogen bonds.
or to the article describing Jmol [5] to the rescue.
Structure
The protein has a 1 alpha chain, that can be seen in pink.
Function
The protein ligand, 9-ODA Image:9-ODA.jpg
Structural highlights
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