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Article type: Research Article
Authors: Paramasivan, Rajaiah | Sivaperumal, Ramamoorthy | Dhananjeyan, Kutty Jegadeeswaran | Thenmozhi, Velayutham | Tyagi, Brij Kishore
Affiliations: Centre for Research in Medical Entomology, (Indian Council of Medical Research), 4, Sarojini Street, Chinna Chokkikulam, Madurai-625002, Tamil Nadu, India | Department of Bioinformatics, Bharathiar University, Coimbatore, Tamil Nadu, India
Note: [] Corresponding author. E-mail: rpsivan2000@yahoo.co.in
Abstract: Olfaction of insects is currently recognized as the major area of research for developing novel control strategies to prevent mosquito-borne infections. A 3-dimensional model (3D) was developed for the salivary gland odorant-binding protein-2 of the mosquito Culex quinquefasciatus, a major vector of human lymphatic filariasis. A homology modeling method was used for the prediction of the structure. For the modeling, two template proteins were obtained by mGenTHERADER, namely the high-resolution X-ray crystallography structure of a pheromone-binding protein (ASP1) of Apis mellifera L., [1R5R:A] and the aristolochene synthase from Penicillium roqueforti [1DI1:B]. By comparing the template protein a rough model was constructed for the target protein using MODELLER, a program for comparative modelling. The structure of OBP of the mosquito Culex quinquefasciatus resembles the structure of pheromone-binding protein ASP1 of Apis mellifera L., [1R5R:A]. From Ramachandran plot analysis it was found that the portion of residues falling into the most favoured regions was 86.0%. The predicted 3-D model may be further used in characterizing the protein in wet laboratory.
Keywords: Salivary odorant-binding protein-2, homology modeling, pheromone-binding protein, aristolochene synthase, Culex quinquefasciatus, 3-D model, MODELLER, mGenTHERADER, X-ray crystallography, predictive model, Swiss-PdbViewer, PROCHECK
Journal: In Silico Biology, vol. 7, no. 1, pp. 1-6, 2007
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