Report

Crystal Structure of the Zα Domain of the Human Editing Enzyme ADAR1 Bound to Left-Handed Z-DNA

See allHide authors and affiliations

Science  11 Jun 1999:
Vol. 284, Issue 5421, pp. 1841-1845
DOI: 10.1126/science.284.5421.1841

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Abstract

The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zα, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zα complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zα 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 Zα to contact Z-DNA.

View Full Text