Mishra S and Gomase VS
Heat shock protein participates in several broad ranges of protein folding processes and control activity of regulatory proteins. Nearly all cells react in a similar manner against the external environmental abrupt changes like heat, chemicals such as analogues of amino acid, ethanol, arsenite, several heavy metals, mitochondrial functional inhibitors, cold, UV light. These all causes several severe, rapid changes in at the level of gene expression. The major significant activity of HSP protein to stabilize newly synthesized protein by securing its right folding, which generally undergone any damaged under cell stress condition. Through overexpression, this protein provides protection to cells against apoptotic cell death. The hsp70 chaperonis targeted as novel anticancer therapeutic candidate for a broad spectrum of tumor types due to its diverse functional role. Homology modeling methodology allowsmodeling the 3Dstructure of the protein using the experimentally determined three dimensional structure of related homologues protein as template. In the current investigation, we have taken the Hsp70 protein and conducted the 3-imensional structure prediction through Swiss- Model by using the crystal structure as the template. Template search of the desired protein were conducted with Blast and HHBlits against the SMTL and keyed out the highest sequence identity, comparatively, above the other obtained template sequences. The homology modelling was performed and the model protein was evaluated by using the PSVS.
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