Odorant Binding by a Pheromone Binding Protein: Active Site Mapping by Photoaffinity Labeling

Biochemistry ◽  
1994 ◽  
Vol 33 (16) ◽  
pp. 4812-4819 ◽  
Author(s):  
Gehua Du ◽  
Chi-Shing Ng ◽  
Glenn D. Prestwich





1978 ◽  
Vol 100 (23) ◽  
pp. 7421-7423 ◽  
Author(s):  
Emil H. White ◽  
H. Mark Perks ◽  
David F. Roswell


2013 ◽  
Vol 796 ◽  
pp. 15-20
Author(s):  
Kai Zun Xu ◽  
Ming Hui Wang ◽  
Lie Ma ◽  
Guo Sheng Li ◽  
Chao Mei ◽  
...  

Bombyx mori pheromone-Binding Protein 1 (BmPBP1) in male moth antennae is a class of Odorant-Binding Proteins (OBPs), it can bind with the specific sex pheromone from female moth, thus initiates the males behaviors like seeking and mating, etc. It has been found that sex pheromone-binding protein 1 is differentially expressed in the antenna of male and female silkworm moths, however, the molecular mechanism of different PBP1 expression and its role in the information transmission are unclear. In this study, we successfully generated the BmPBP1 polyclonal antibody and used it to detect BmPBP1 expression in the silkworm moth antenna. Thus this work is helpful for further studies on the function of BmPBP1 in the information communication between male and female moths.



1989 ◽  
Vol 260 (2) ◽  
pp. 601-604 ◽  
Author(s):  
M Leyh-Bouille ◽  
J Van Beeumen ◽  
S Renier-Pirlot ◽  
B Joris ◽  
M Nguyen-Distèche ◽  
...  

The N-terminal region of the Streptomyces K15 DD-peptidase/penicillin-binding protein shows high homology with that of other penicillin-interactive proteins or domains. The active-site serine residue of the conserved tetrad Ser-Xaa-Xaa-Lys occurs at position 35. There is no indication for the presence of a signal peptide or an N-terminal hydrophobic sequence, suggesting that the Streptomyces K15 enzyme is probably anchored to the membrane by a C-terminal peptide segment.



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