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International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 23.3, pp. 588-622
https://doi.org/10.1107/97809553602060000716 Chapter 23.3. Nucleic acids
a
Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095–1570, USA |
Footnotes
1
Rich and co-workers (Schwartz et al., 1999![[link]](/graphics/greenarr.gif)
) have recently solved the crystal structure of the Zα domain of the human editing enzyme ADAR1 in a complex with a six-base-pair Z-DNA helix of sequence CGCGCG. This left-handed hexamer may suffer from the same length versus conformation uncertainty mentioned later in this chapter in connection with oligonucleotide crystals, especially since protein–DNA contacts in the Zα complex occur only with the zigzag phosphate backbone, which is not that dissimilar in Z-DNA (Fig. 23.3.3.3) and Z(WC)-DNA (Fig. 23.3.3.7). Nevertheless, it is encouraging to see a short segment of Z actually making contact with its protein in a presumably biologically relevant context.
) have recently solved the crystal structure of the Zα domain of the human editing enzyme ADAR1 in a complex with a six-base-pair Z-DNA helix of sequence CGCGCG. This left-handed hexamer may suffer from the same length versus conformation uncertainty mentioned later in this chapter in connection with oligonucleotide crystals, especially since protein–DNA contacts in the Zα complex occur only with the zigzag phosphate backbone, which is not that dissimilar in Z-DNA (Fig. 23.3.3.3) and Z(WC)-DNA (Fig. 23.3.3.7). Nevertheless, it is encouraging to see a short segment of Z actually making contact with its protein in a presumably biologically relevant context.