Homology Modeling and Docking Studies of Cold Shock Protein Homologs (Isoforms) of E. coli
Under the environmental stress condition, protein folding or refolding has become an important issue for the
survival of any microorganism. In majority of bacteria, such as Escherichia coli, temperature downshift leads to a transient
arrest of cell growth, which results in inhibition of general protein synthesis. However, syntheses of a number of proteins,
called cold-shock proteins are induced under these conditions. These proteins minimize secondary structure folding
and acts as DNA or RNA chaperons. In the present study, to understand the mechanism of CSPs and to identify the key
residues involved in nucleic acid binding, we generated homology model of cold shock protein homologs from CspB to
CspI of Escherichia coli using Modeler 9v1. The modeled homologs were docked with potential ligand and protein-ligand
interactions were studied using program, GLIDE. Docking results revealed that several basic and aromatic amino acid
residues are conserved on the ligand binding surface of CSP homolog and aromatic residues that are essentially required
for nucleic acid binding, also play important role in protein stability and protein folding inhibition.
Keywords: Homology modeling, Molecular docking, Cold shock protein, GLIDE, Escherichia coli.
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