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. Author manuscript; available in PMC: 2014 Sep 4.
Published in final edited form as: Nat Genet. 2012 Sep 23;44(11):1243–1248. doi: 10.1038/ng.2414

Figure 2.

Figure 2

Structural context of ADAR1 protein substitutions. (a) The surface of the ADAR domain (dark pink) with surface substitutions highlighted in bright pink. The active site contains a zinc ion (black) in the center. Arg892His, Lys999Asn, Gly1007Arg, Tyr1112Phe and Asp1113His are all on the same side of the domain as the active site, and all have the potential to alter charge and/or hydrogen bonding characteristics of the surface in the region that is likely to be responsible for RNA binding. (b,c) Models of wild-type (b) and mutant (c) residues at position 870 in the ADAR domain. Interactions between the residue and the surrounding protein structure are indicated by all-atom contact dots (blue). Green dots represent energetically favorable van der Waals interactions, whereas red and pink spikes indicate unfavorable van der Waals overlaps. The Ile872Thr substitution introduces an unsatisfied hydrogen bond donor/acceptor group, which is destabilizing but not easily depicted. (d,e) Interactions of the proline residue at position 193 (Pro193) in the Z-DNA–binding domain (d). Contact dots (blue, green, yellow) indicate favorable interactions between Pro193 and the DNA backbone (white). These interactions are absent in the mutant form (e). (f) Modeling of the deaminase domain of ADAR2 suggests contact with dsRBD2 close to Gly1007, highlighting the possibility for an arginine residue to make functionally important polyvalent interactions.