The computational view inside the dynamical behavior of the RNA-binding motive
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| Year of publication | 2010 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | The members of an enzyme family known as ADARs (adenosine deaminases that act on RNA) play a crucial role in the RNA editing process in all organisms. ADARs target double-stranded regions of nuclear-encoded RNA (dsRNA). 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. We focus on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Molecular dynamics (MD) techniques are capable of providing detailed insight into the motions that occur during molecular recognition and how motional properties change upon binding. MD and NMR techniques synergistically reinforce each other when applied to the same system. Our goal in this work is to explain the role of mismatches and their flexibility for the ADAR2-dsRNA complex. |
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