Figure 8 | Scientific Reports

Figure 8

From: PKR activity modulation by phosphomimetic mutations of serine residues located three aminoacids upstream of double-stranded RNA binding motifs

Figure 8

Model: Ser6 and Ser97 mutations impact the stability of the closed PKR conformation. (a) Wild type PKR: dsRNA binding by DRBM1 and/or DRBM2 destabilizes the interaction between the RNA binding domain and the kinase domain, leading to opening, dimerization, autophosphorylation and activation of the kinase activity. (b) The Ser-to-Ala mutations spontaneously destabilize the close conformation and facilitate opening of PKR upon dsRNA binding. (c) Ser6 and 97 phosphorylation or Ser-to-Asp phosphomimetic mutations prevent neither dsRNA binding nor dimerization but likely contribute to maintain PKR in a close, inactive conformation.

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