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NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes
- Authors
- Lee, Ae-Ree; Kim, Hee-Eun; Lee, Yeon-Mi; Jeong, Minjee; Choi, Kwang-Ho; Park, Jin-Wan; Choi, Yong-Geun; Ahn, Hee-Chul; Choi, Byong-Seok; Lee, Joon-Hwa
- Issue Date
- 9-Nov-2012
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- NMR; Z-DNA; Backbone dynamics; Z-DNA binding protein; DNA-protein interaction
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.428, no.1, pp 137 - 141
- Pages
- 5
- Indexed
- SCI
SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 428
- Number
- 1
- Start Page
- 137
- End Page
- 141
- ISSN
- 0006-291X
1090-2104
- Abstract
- The Z-DNA binding domain of human ADAR1 (Z alpha(ADAR1)) 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 Z alpha(ADAR1) 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 Z alpha(ADAR1) initially binds to d(CGCGCG)(2) through the distinct conformation, especially in the unusually flexible beta 1-loop-alpha 2 region, from the d(CGCGCG)(2)-(Z alpha(ADAR1))(2) complex. This study also suggests that Z alpha(ADAR1) 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. 2012 Elsevier Inc. All rights reserved.
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