Abstract
The Z-DNA binding domain of human ADAR1 (ZαADAR1) preferentially binds Z-DNA rather than B-DNA with high binding affinity. Here, we have carried out chemical shift perturbation and backbone dynamics studies of ZαADAR1 in the free form and in complex with three DNA duplexes, d(CGCGCG)2, d(CACGTG)2, and d(CGTACG)2. This study reveals that ZαADAR1 initially binds to d(CGCGCG)2 through the distinct conformation, especially in the unusually flexible β1-loop-α2 region, from the d(CGCGCG)2-(ZαADAR1)2 complex. This study also suggests that ZαADAR1 exhibits a distinct conformational change during the B-Z transition of non-CG-repeat DNA duplexes with low binding affinities compared to the CG-repeat DNA duplex.
Original language | English |
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Pages (from-to) | 137-141 |
Number of pages | 5 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 428 |
Issue number | 1 |
DOIs | |
State | Published - 9 Nov 2012 |
Keywords
- Backbone dynamics
- DNA-protein interaction
- NMR
- Z-DNA
- Z-DNA binding protein