Computational Analysis of HSP-60 Protein with Structural Insights into Chaperonin Containing TCP-1 Subunit 5 in Bos Taurus

Abstract

Heat shock protein 60 kDa (HSP60) is a crucial chaperone that guides appropriate folding of denatured proteins under heat stress conditions. HSP60 provides assistance in correct folding of a multitude of denatured proteins. The Group II eukaryotic chaperonin TCP-1 ring complex is (TRiC or CCT) important cytosolic chaperonin which plays important role in folding of essential subset of cytosolic proteins and is believed to be highly conserved among different eukaryotic species. In this study, an extensive in silico analysis has been performed ranging from sequence comparison among species to homology modeling of Bos taurus Cct5 protein and determination of Hsp60 interacting partners. The comparative analysis of the protein revealed certain significant variations in Bos taurus. The experimental protein structure for Cct5 in Bos taurus is unknown till date, therefore the putative protein structure was determined using homology modeling. The stereo chemical properties of protein were assessed by utilizing several scrutiny tools such as PROCHECK, VERIFY3D and RAMPAGE to ensure model accuracy. The mode of interaction between HSF1 and Cct5 protein was evaluated by molecular docking studies.