Key result
Recent X-ray crystal structures of the human ADAR2 deaminase domain bound to RNA editing substrates reveal how these enzymes bind RNA and promote adenosine deamination.
This review elucidates the structural basis for how ADARs bind RNA and promote adenosine deamination, providing models for substrate recognition.
Deamination of adenosine in RNA to form inosine has wide ranging consequences on RNA function including amino acid substitution to give proteins not encoded in the genome. What determines which adenosines in an mRNA are subject to this modification reaction? The answer lies in an understanding of the mechanism and substrate recognition properties of adenosine deaminases that act on RNA (ADARs). Our recent publication of X-ray crystal structures of the human ADAR2 deaminase domain bound to RNA editing substrates shed considerable light on how the catalytic domains of these enzymes bind RNA and promote adenosine deamination. Here we review in detail the deaminase domain-RNA contact surfaces and present models of how full length ADARs, bearing double stranded RNA-binding domains (dsRBDs) and deaminase domains, could process naturally occurring substrate RNAs.
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Thomas et al. (2017) conducted a review in RNA editing by ADARs. ADARs (adenosine deaminases that act on RNA) was evaluated. Recent X-ray crystal structures of the human ADAR2 deaminase domain bound to RNA editing substrates reveal how these enzymes bind RNA and promote adenosine deamination.
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