Conformational exchange of the Zalpha domain of human RNA editing enzyme ADAR1 studied by NMR spectroscopy
Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune responses, and viral infections. Numerous studies have implicated a role for conformational motions during ZBPs binding upon DNA, but the quantitative intrinsic conformational exchanges of ZBP have not been elucidated. To understand the correlation between the biological function and dynamic feature of the Z? domains of human ADAR1 (hZ?(ADAR1)), we have performed the ^(15)N backbone amide Carr-Purcell-Meiboom-Gill...
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