| First Author | Schwartz T | Year | 1999 |
| Journal | Science | Volume | 284 |
| Issue | 5421 | Pages | 1841-5 |
| PubMed ID | 10364558 | Mgi Jnum | J:55693 |
| Mgi Id | MGI:1339216 | Doi | 10.1126/science.284.5421.1841 |
| Citation | Schwartz T, et al. (1999) Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA. Science 284(5421):1841-5 |
| abstractText | 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. |
