NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.
 

NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.

http://www.bionmr.com//www.ncbi.nlm....PubMedLink.gif Related Articles NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.

Biochem Biophys Res Commun. 2012 Nov 9;428(1):137-41

Authors: Lee AR, Kim HE, Lee YM, Jeong M, Choi KH, Park JW, Choi YG, Ahn HC, Choi BS, Lee JH

Abstract
The Z-DNA binding domain of human ADAR1 (Z?(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?(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?(ADAR1) initially binds to d(CGCGCG)(2) through the distinct conformation, especially in the unusually flexible ?1-loop-?2 region, from the d(CGCGCG)(2)-(Z?(ADAR1))(2) complex. This study also suggests that Z?(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.


PMID: 23079620 [PubMed - indexed for MEDLINE]



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