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

Abstract：

:The Z-DNA binding domain of human ADAR1 (Zα(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 Zα(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 Zα(ADAR1) initially binds to d(CGCGCG)(2) through the distinct conformation, especially in the unusually flexible β1-loop-α2 region, from the d(CGCGCG)(2)-(Zα(ADAR1))(2) complex. This study also suggests that Zα(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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

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

doi

10.1016/j.bbrc.2012.10.026

subject

Has Abstract

pub_date

2012-11-09 00:00:00

pages

137-41

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)01963-8

journal_volume

428

pub_type

杂志文章

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