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

Ae Ree Lee, Hee Eun Kim, Yeon Mi Lee, Minjee Jeong, Kwang Ho Choi, Jin Wan Park, Yong Geun Choi, Hee Chul Ahn, Byong Seok Choi, Joon Hwa Lee

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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 languageEnglish
Pages (from-to)137-141
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume428
Issue number1
DOIs
StatePublished - 9 Nov 2012

Keywords

  • Backbone dynamics
  • DNA-protein interaction
  • NMR
  • Z-DNA
  • Z-DNA binding protein

Fingerprint

Dive into the research topics of 'NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes'. Together they form a unique fingerprint.

Cite this