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. Author manuscript; available in PMC: 2016 Nov 10.
Published in final edited form as: Biochemistry. 2015 Oct 26;54(44):6663–6672. doi: 10.1021/acs.biochem.5b01046

Figure 4. Schematic of formation of the kinase domain dimer.

Figure 4

The kinase domain is depicted in green, dsRBD1 in blue and dsRBD2 in red. The fluorophore is depicted as an orange star. Upon binding of two pAz-F261-A488 monomers to a single dsRNA the kinase domains may dimerize in the back-to-back parallel configuration, leading to homo-FRET (top). Alternatively, the protein may bind to the dsRNA in a configuration that does not support kinase domain dimerization that leads to homo-FRET (bottom). The term RP2 encompasses all forms of the RNA containing two bound PKR monomers.