Logo image
Pheromone discrimination by the Pheromone-Binding protein of Bombyx mori
Journal article   Peer reviewed

Pheromone discrimination by the Pheromone-Binding protein of Bombyx mori

F. Gräter, W. Xu, W. Leal and H. Grubmüller
Structure, Vol.14(10), pp.1577-1586
2006
url
Link to Published Version *Subscription may be requiredView

Abstract

Pheromone-binding proteins are postulated to contribute to the exquisite specificity of the insect's olfactory system, acting as a filter by preferentially binding only one of the components of the natural pheromone. Here, we investigated the possible discrimination of the two very similar components of the natural pheromone gland from the silk moth, Bombyx mori, bombykol and bombykal, by the only pheromone-binding protein (BmorPBP) known to be expressed in the pheromone-detecting sensilla. Free-energy calculations and virtual docking indicate that both bombykol and bombykal bind to BmorPBP with similar affinity. In addition, in vitro competitive binding assays showed that both bombykol and bombykal were bound by BmorPBP with nearly the same high affinity. While BmorPBP might filter out other physiologically irrelevant compounds hitting the sensillar lymph, discrimination between the natural pheromone compounds must be achieved by molecular interactions with their cognate receptors.

Details

UN Sustainable Development Goals (SDGs)

This output has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

Source: InCites

Metrics

InCites Highlights

These are selected metrics from InCites Benchmarking & Analytics tool, related to this output

Collaboration types
Domestic collaboration
International collaboration
Citation topics
3 Agriculture, Environment & Ecology
3.220 Smell & Taste Science
3.220.701 Olfactory Systems
Web Of Science research areas
Biochemistry & Molecular Biology
Biophysics
Cell Biology
ESI research areas
Biology & Biochemistry
Logo image