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. Author manuscript; available in PMC: 2012 Feb 1.
Published in final edited form as: Curr Opin Struct Biol. 2010 Dec 8;21(1):119–127. doi: 10.1016/j.sbi.2010.11.003

Figure 2.

Figure 2

Structural biology of PKR. (a) Structures of the two domains of PKR. PKR is a 551 amino acid protein that contains an N-terminal dsRNA binding domain (dsRBD) that is comprised of two dsRNA binding motifs (dsRBMs) spaced by a flexible 20 amino acid linker depicted below the dsRBMs, and a C-terminal kinase domain with small and large N- and C-terminal domains. Available are an NMR structure of the dsRBD (pdbid 1QU6) and a crystal structure of the kinase domain complexed with eIF2α substrate (eIF2α omitted here). The kinase crystallizes as a dimer (pdbid 2A1A). (b) Structure of a dsRBM from X. laevis rbpa bound to dsRNA (pdbid 1DI2) [16]. The dsRNA is 10 bp in length, and two helices are shown stacked end-to-end. Each dsRBM occupies one face of the dsRNA, and packing occurs along different faces of the dsRNA. Shown are side-on and end-on views.