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Schade, M., Turner, C. J., Kuhne, R., Schmieder, P., Lowenhaupt, K., Herbert, A., Rich, A., Oschkinat, H. (1999) The solution structure of the Zalpha 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 doi:10.1073/pnas.96.22.12465

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Reference TypeJournal (article/letter/editorial)
TitleThe solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA
JournalProceedings of the National Academy of Sciences
AuthorsSchade, M.Author
Turner, C. J.Author
Kuhne, R.Author
Schmieder, P.Author
Lowenhaupt, K.Author
Herbert, A.Author
Rich, A.Author
Oschkinat, H.Author
Year1999 (October 26)Volume96
Issue22
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.96.22.12465Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1630679Long-form Identifiermindat:1:5:1630679:6
GUID0
Full ReferenceSchade, M., Turner, C. J., Kuhne, R., Schmieder, P., Lowenhaupt, K., Herbert, A., Rich, A., Oschkinat, H. (1999) The solution structure of the Zalpha 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 doi:10.1073/pnas.96.22.12465
Plain TextSchade, M., Turner, C. J., Kuhne, R., Schmieder, P., Lowenhaupt, K., Herbert, A., Rich, A., Oschkinat, H. (1999) The solution structure of the Zalpha 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 doi:10.1073/pnas.96.22.12465
In(1999, October) Proceedings of the National Academy of Sciences Vol. 96 (22) Proceedings of the National Academy of Sciences

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Brown, B. A., Lowenhaupt, K., Wilbert, C. M., Hanlon, E. B., Rich, A. (2000) The Zalpha domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA. Proceedings of the National Academy of Sciences, 97 (25) 13532-13536 doi:10.1073/pnas.240464097
Kahmann, J. D., Wecking, D. A., Putter, V., Lowenhaupt, K., Kim, Y.-G., Schmieder, P., Oschkinat, H., Rich, A., Schade, M. (2004) The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro. Proceedings of the National Academy of Sciences, 101 (9) 2712-2717 doi:10.1073/pnas.0308612100
Herbert, A., Alfken, J., Kim, Y.-G., Mian, I. S., Nishikura, K., Rich, A. (1997) A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase. Proceedings of the National Academy of Sciences, 94 (16) 8421-8426 doi:10.1073/pnas.94.16.8421
Herbert, A. G., Spitzner, J. R., Lowenhaupt, K., Rich, A. (1993) Z-DNA binding protein from chicken blood nuclei. Proceedings of the National Academy of Sciences, 90 (8) 3339-3342 doi:10.1073/pnas.90.8.3339
Herbert, A., Rich, A. (2001) The role of binding domains for dsRNA and Z-DNA in the in vivo editing of minimal substrates by ADAR1. Proceedings of the National Academy of Sciences, 98 (21) 12132-12137 doi:10.1073/pnas.211419898
Herbert, A., Lowenhaupt, K., Spitzner, J., Rich, A. (1995) Chicken double-stranded RNA adenosine deaminase has apparent specificity for Z-DNA. Proceedings of the National Academy of Sciences, 92 (16) 7550-7554 doi:10.1073/pnas.92.16.7550
Ha, S. C., Kim, D., Hwang, H.-Y., Rich, A., Kim, Y.-G., Kim, K. K. (2008) The crystal structure of the second Z-DNA binding domain of human DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to Z-DNA. Proceedings of the National Academy of Sciences, 105 (52) 20671-20676 doi:10.1073/pnas.0810463106
Athanasiadis, Alekos, Placido, Diana, Maas, Stefan, Brown, Bernard A., Lowenhaupt, Ky, Rich, Alexander (2005) The Crystal Structure of the Zβ Domain of the RNA-editing Enzyme ADAR1 Reveals Distinct Conserved Surfaces Among Z-domains. Journal of Molecular Biology, 351 (3). 496-507 doi:10.1016/j.jmb.2005.06.028
Kelly, M. J. S., Ball, L. J., Krieger, C., Yu, Y., Fischer, M., Schiffmann, S., Schmieder, P., Kuhne, R., Bermel, W., Bacher, A., Richter, G., Oschkinat, H. (2001) The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site. Proceedings of the National Academy of Sciences, 98 (23) 13025-13030 doi:10.1073/pnas.231323598
Patzelt, H., Simon, B., terLaak, A., Kessler, B., Kuhne, R., Schmieder, P., Oesterhelt, D., Oschkinat, H. (2002) The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy. Proceedings of the National Academy of Sciences, 99 (15) 9765-9770 doi:10.1073/pnas.132253899
Brown, Bernard A., Athanasiadis, Alekos, Hanlon, Eugene B., Lowenhaupt, Ky, Wilbert, Christina M., Rich, Alexander (2002) Crystallization of the Zα domain of the human editing enzyme ADAR1 complexed with a DNA–RNA chimeric oligonucleotide in the left-handed Z-conformation. Acta Crystallographica Section D Biological Crystallography, 58 (1). 120-123 doi:10.1107/s0907444901013312
 
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