Nowadays climate changes and wide usage of chemical insecticides causes the emergence of Anopheles mosquito resistant species and environmental hazards. Therefore, biocontrol as alternative approache provides the vivid outlook for combating these risks. Hereupon the special attention is paid to insecticides bacteria especially Bacillus thuringiensis and protein derived from it as Cry toxins. However, scrutinizing the structural and functional characteristics of these toxins have not been much attended, so it is aimed in this study by in silico investigations. For this purpose Cry4, Cry11, Cry19, Cry24 and Cry39 protein sequences were extracted from NCBI database, monitoring structural and functional, physicochemical, topological features, prediction of secondary and three-dimensional modelling was carried out with programs like Interproscan, Protparam, TMHMM, Psipred and modeller9.15. Finally, their binding affinity with relevant receptors was assessed by PatchDock molecular docking program. The results indicate various features of physicochemical, non-secretory and toxin accumulation. Functional monitoring has traced domains with similar functions of other Cry toxin family members. Secondary structure prediction shows the existence of both helixes and sheets in similar distribution pattern with each other. In addition, the design and quality evaluation of 3D structure of all toxins were obtained in desirable level. The binding affinity assessment represents stronger binding of Cry11 and Cry24 to most of the receptors. In general, the results of this study in addition of provision functional data related to Cry toxin, provide optimum practical model of capable toxins production based on multimodal protein design for biocontrol of Malaria mosquitos.

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