期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1999
卷号：96
期号：22
页码：12465-12470
DOI：10.1073/pnas.96.22.12465
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain Z. Here we report the solution structure of free Z and map the interaction surface with Z-DNA, confirming roles previously assigned to residues by mutagenesis. Comparison with the crystal structure of the (Z)2/Z-DNA complex shows that most Z-DNA contacting residues in free Z are prepositioned to bind Z-DNA, thus minimizing the entropic cost of binding. Comparison with homologous (+{beta})helix-turn-helix/B-DNA complexes suggests that binding of Z to B-DNA is disfavored by steric hindrance, but does not eliminate the possibility that related domains may bind to both B- and Z-DNA.
