 On the cover: To advertise their readiness to mate, female moths release minute amounts of sex pheromones. With tens of thousands of tiny hairs on the antennae, males can rapidly detect these scents even from a distance. Pheromone-binding proteins are essential for the fast response to pheromones and for detecting the readiness of a mate for reproduction. Art by Steve Oerding, UC Davis (Text courtesy of Structure) |
Structure Journal, Volume 15 Issue 9: September 11, 2007
Authors:
Catherine Lautenschlager, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School
Walter S. Leal, Department of Entomology, University of California, Davis
Jon Clardy, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School
SUMMARY
Insect pheromone-binding proteins (PBPs)
transport sex pheromones through the aqueous
layer surrounding G protein-coupled receptors
that initiate signaling events leading to
mating. This PBP-receptor system strongly discriminates
between ligands with subtle structural
differences, but it has proved difficult to
distinguish the degree of discrimination of the
PBP from that of the G protein-coupled receptor.
The three-dimensional structures of the
PBP of Bombyx mori, the silkworm moth, both
with and without its cognate ligand bombykol
([E,Z]-10,12-hexadecadienol), have been determined
by X-ray crystallography and NMR. In
this paper, the structures of the same binding
protein with bound iodohexadecane and bell
pepper odorant were determined at 1.9 and
2.0 A°
, respectively. These structures illustrate
the remarkable plasticity in the ligand binding
site of the PBP, but suggest the protein might
still act as a filter during pheromone signal
processing.
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-Kathy Keatley Garvey
Communications Specialist
Department of Entomology
(530) 754-6894
