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- Title
Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA.
- Authors
Schwartz, T; Rould, M A; Lowenhaupt, K; Herbert, A; Rich, A
- Abstract
The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA.
- Publication
Science (New York, N.Y.), 1999, Vol 284, Issue 5421, p1841
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.284.5421.1841