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Issue:ISSN 2095-1353
           CN 11-6020/Q
Director:Chinese Academy of Sciences
Sponsored by:Chinese Society of Entomological;institute of zoology, chinese academy of sciences;
Address:Chaoyang District No. 1 Beichen West Road, No. 5 hospital,Beijing City,100101, China
Your Position :Home->Past Journals Catalog->2017年54 No.6

Modeling the odorant binding protein of the red palm weevil, Rhynchophorus ferrugineus
Author of the article:YAN Wei1, 2** LUO You-Qing1*** LI Chao-Xu2 LIU Li2 QIN Wei-Quan2 PENG Zheng-Qiang3
Author's Workplace:1. The Key Laboratory of Beijing for Control to Forest Pest, Beijing Forestry University, Beijing 100083, China; 2. Coconut Research Institute, Chinese Academy of Tropical Agricultural Sciences, Wenchang 571339, China; 3. Environment and Plant Protection Institute, Chinese Academy of Tropical Agricultural Sciences, Haikou 571101, China
Key Words:odorant binding protein, homology modeling, three dimensional structure, Rhynchophorus ferrugineus

 [Objectives]  To obtain the three-dimensional structure of the odorant binding protein (OBP) of the red palm weevil, Rhynchophorus ferrugineus, a notorious invasive pest, in order to develop potential volatile compounds to control this weevil based on the computational reverse chemical ecology approach. [Methods]  Two, three dimensional structures of R. ferrugineus were homologically modeled based on crystal structures of OBPs from other insects that have been deposited in the Protein Data Bank (PDB). The modeled structures were evaluated by Procheck, VERIFY_3D and ERRAT and their evaluation scores indicate that model quality is high. [Results]  The two, modeled, putative, three-dimensional, R. ferrugineus OBPs were composed of 6 α helixes and rebounds connecting the helixes. Three pairs of disulfide bonds formed by 6 cysteines were the key to their structural stability. [Conclusion]  These modeled OBP structures lay a foundation for the future screening of potential active volatiles to control R. ferrugineus by molecular docking. 

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