Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity

@inproceedings{Matthews2016StructuresOH,
  title={Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity},
  author={Melissa M. Matthews and Justin M. Thomas and Yuxuan Zheng and Kiet Ve Tran and Kelly J. Phelps and Anna I. Scott and Jocelyn Havel and Andrew J Fisher and Peter A. Beal},
  booktitle={Nature Structural &Molecular Biology},
  year={2016}
}
Adenosine deaminases acting on RNA (ADARs) are editing enzymes that convert adenosine to inosine in duplex RNA, a modification reaction with wide-ranging consequences in RNA function. Understanding of the ADAR reaction mechanism, the origin of editing-site selectivity, and the effect of mutations is limited by the lack of high-resolution structural data for complexes of ADARs bound to substrate RNAs. Here we describe four crystal structures of the human ADAR2 deaminase domain bound to RNA… CONTINUE READING