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The P58IPK, an endogenous PKR inhibitor from the tetratricopeptide repeat (TPR) family, contains nine tandemly arranged repeats (TPR1-9) of 34 amino acids at the N-terminus. The homology between its C-terminal domain and the J domain of the DnaJ heat shock proteins also makes P58IPK a member of the HSP family of proteins. The P58IPK can inhibit PKR by direct binding and interruption in PKR dimerization. The PKR binding domain of P58IPK has been mapped to its TPR6 motif. Both NP and Hsp40 share a common binding site on P58IPK. And NP competes with Hsp40 for binding to P58IPK, will lead to the dissociation of Hsp40-P58IPK complex.