NMR study of the Z-DNA binding mode and B-Z transition activity of the Zα domain of human ADAR1 when perturbed by mutation on the α3 helix and β-hairpin.

Minjee Jeong,Ae-Ree Lee,Hee-Eun Kim,Yong-Geun Choi,Byong-Seok Choi,Joon-Hwa Lee

Archives of Biochemistry and Biophysics（2014）

引用 9|浏览6

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摘要

•K169A, K170A, and Y177I mutants exhibit conformational change in hydrophobic faces.•K170A, R174A, and W195F mutations slightly affect the Z-DNA binding affinity.•K170A and R174A mutants induce significant destabilization of the G2·C5 base pair.

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关键词

NMR,Z-DNA,Hydrogen exchange,ADAR1,B–Z transition,DNA–protein interactions

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