RNA editing in disease: mechanisms and therapeutic potential

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FIGURE 1.
FIGURE 1.

Mammalian ADARs. All ADARs are characterized by a C-terminal catalytic domain. In ADAR3, the deaminase domain is inactive. dsRBDs are required for recognizing double-stranded substrate RNA. ADAR1 has a nuclear localization signal (NLS) flanking its third dsRBD, and ADAR1p150 has an N-terminal nuclear export signal. Consequently, ADAR1 is manly cytoplasmic, while all other ADARs are primarily nuclear. A Zα domain can bind RNAs in Z-conformation in ADAR1p150, while the Zβ domain found in ADAR1p150 and p110 is degenerate.

This Article

  1. RNA 31: 359-368