Ontology highlight
ABSTRACT:
SUBMITTER: Macbeth MR
PROVIDER: S-EPMC1850959 | biostudies-literature | 2005 Sep
REPOSITORIES: biostudies-literature
Science (New York, N.Y.) 20050901 5740
We report the crystal structure of the catalytic domain of human ADAR2, an RNA editing enzyme, at 1.7 angstrom resolution. The structure reveals a zinc ion in the active site and suggests how the substrate adenosine is recognized. Unexpectedly, inositol hexakisphosphate (IP6) is buried within the enzyme core, contributing to the protein fold. Although there are no reports that adenosine deaminases that act on RNA (ADARs) require a cofactor, we show that IP6 is required for activity. Amino acids ...[more]