Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain Zα. Here we report the solution structure of free Zα and map the interaction surface with Z-DNA, confirming roles previously assigned to residues by mutagenesis. Comparison with the crystal structure of the (Zα) 2 /Z-DNA complex shows that most Z-DNA contacting residues in free Zα are prepositioned to bind Z-DNA, thus minimizing the entropic cost of binding. Comparison with homologous (α+β)helix–turn–helix/B-DNA complexes suggests that binding of Zα 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.

Bibliography

Schade, M., Turner, C. J., Kühne, R., Schmieder, P., Lowenhaupt, K., Herbert, A., Rich, A., & Oschkinat, H. (1999). The solution structure of the Zα domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA. Proceedings of the National Academy of Sciences, 96(22), 12465–12470.

Authors 8
  1. Markus Schade (first)
  2. Christopher J. Turner (additional)
  3. Ronald Kühne (additional)
  4. Peter Schmieder (additional)
  5. Ky Lowenhaupt (additional)
  6. Alan Herbert (additional)
  7. Alexander Rich (additional)
  8. Hartmut Oschkinat (additional)
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Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 10:35 a.m.)
Deposited 3 years, 2 months ago (June 7, 2022, 12:17 a.m.)
Indexed 2 months, 3 weeks ago (June 6, 2025, 6:44 a.m.)
Issued 25 years, 10 months ago (Oct. 26, 1999)
Published 25 years, 10 months ago (Oct. 26, 1999)
Published Online 25 years, 10 months ago (Oct. 26, 1999)
Published Print 25 years, 10 months ago (Oct. 26, 1999)
Funders 0

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@article{Schade_1999, title={The solution structure of the Zα domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA}, volume={96}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.96.22.12465}, DOI={10.1073/pnas.96.22.12465}, number={22}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Schade, Markus and Turner, Christopher J. and Kühne, Ronald and Schmieder, Peter and Lowenhaupt, Ky and Herbert, Alan and Rich, Alexander and Oschkinat, Hartmut}, year={1999}, month=oct, pages={12465–12470} }