title: ADAR proteins: structure and catalytic mechanism.
abstract: Since the discovery of the adenosine deaminase (ADA) acting on RNA (ADAR) family of proteins in 1988 (Bass and Weintraub, Cell 55:1089-1098, 1988)   (Wagner et al. Proc Natl Acad Sci U S A 86:2647-2651, 1989), we have learned much about their structure and catalytic mechanism. However, much about these enzymes is still unknown, particularly regarding the selective recognition and processing of specific adenosines within substrate RNAs. While a crystal structure of the catalytic domain of human ADAR2 has been solved, we still lack structural data for an ADAR catalytic domain bound to RNA, and we lack any structural data for other ADARs. However, by analyzing the structural data that is available along with similarities to other deaminases, mutagenesis and other biochemical experiments, we have been able to advance the understanding of how these fascinating enzymes function.
authors.affiliation: Department of Chemistry, University of California, One Shields Ave, Davis, CA 95616, USA.
authors.forename: Rena A
authors.initials: RA
authors.lastname: Goodman
authors.forename: Mark R
authors.initials: MR
authors.lastname: Macbeth
authors.forename: Peter A
authors.initials: PA
authors.lastname: Beal
mesh_terms: D000243:Adenosine Deaminase / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D055162:Biocatalysis; D006801:Humans; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D016601:RNA-Binding Proteins; D015032:Zinc / Q000737:chemistry
chemical_list: D016601:RNA-Binding Proteins; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase; D015032:Zinc