Fig. 1: Three-dimensional modeling analysis of ADAR1 oligomerization.
From: High-speed atomic force microscopy and 3D modeling reveal the structural dynamics of ADAR1 complexes
a Illustration of the domain arrangement of ADAR1 isoforms (p150:1226 aa and p110: 931 aa). b The ADAR1 dimer model predicted two distinct interfaces, named interface x (IFx) and interface y (IFy) on each deaminase domain. The IFx (Pro826-Pro834; Asp877-Asp880; Ser932-Val955) and IFy (Gly1183-Asp1205) shown in red and green colors, respectively, are complementary and contact each other. A total of 4 hydrogen bonds formed between four residue pairs in the IFx and IFy regions contribute to monomer-monomer interactions within the dimer model (inset, magnified). c Computational models of ADAR1 oligomerization highlight the complementary interactions between IFx and IFy across monomers, suggesting a mechanism for the higher-order organization of ADAR1.
