Homology modeling and in-silico substrate binding analysis of Enterotoxigenic Escherichia coli chaperones

The Pathogenic strains of Escherichia coli are always one of the major causes of infections in developing countries. The fimbriaes on the surface of E.coli mediate microbial attachment to host cells and are important virulence factors [1-2]. Chaperones and usher proteins involved in the biogenesis of the major fimbriae [3]. Our studied showed significant similarities in physicochemical properties of chaperons and also fimbrial subunits among different strain of E.coli. The 3D-structures of 20 molecules chaperone and fimbriae subunit were modeled using Modeller 9v20 [4]. The quality of the models were assessed using PROCHECK, Verify3D and ProSA II.The castp and FTsite servers were used for prediction of interactive sites of proteins. The information of interactive pocket were used for fimbriae subunits and chaperone docking.The physicochemical properties and 3-D structures of interaction pockets of chaperones were compared and result detected significantes similarities among various chaperones .Now we are looking for the inhibitors to block the chaperon-fimbriae major subunit interaction sites. The resulting inhibitors could be introduce as drug candidates.

کلیدواژه ها:

Fimbriae ، Chaperone ، Molecular Modeller