Publication details
The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
| Authors | |
|---|---|
| Year of publication | 2009 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | Like RNA splicing, RNA editing alters the sequence of an RNA from that encoded in the DNA. Typically, a single RNA splicing reaction removes a large block of contiguous sequence, whereas each RNA editing reaction changes only one or two nucleotides. Therefore splicing is a cut-and-paste mechanism whereas editing is one of fine-tuning. RNA editing by adenosine deamination is catalyzed by members of an enzyme family known as adenosine deaminases that act on RNA (ADARs). ADARs are RNA editing enzymes that target double-stranded regions of nuclear-encoded RNA. ADARs are also interesting in regard to the remarkable double-stranded structures of their substrates and how enzyme specificity is achieved with little regard to sequence. ADARs from all organisms have a common domain structure that includes variable numbers of double-stranded RNA (dsRNA) binding motifs (dsRBMs) followed by a highly conserved C-terminal catalytic domain. We focused on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Using MD simulations, we study the role of mismatches and their flexibility for the formation of dsRBM-RNA complexes. |
| Related projects: |
|