title: ADAR proteins: double-stranded RNA and Z-DNA binding domains.
abstract: Adenosine deaminases acting on RNA (ADAR) catalyze adenosine to inosine editing within double-stranded RNA (dsRNA) substrates. Inosine is read as a guanine by most cellular processes and therefore these changes create codons for a different amino acid, stop codons or even a new splice-site allowing protein diversity generated from a single gene. We review here the current structural and molecular knowledge on RNA editing by the ADAR family of protein. We focus especially on two types of nucleic acid binding domains present in ADARs, namely the dsRNA and Z-DNA binding domains.
authors: Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zürich, Switzerland.
authors: Pierre
authors: P
authors: Barraud
authors: Frédéric H-T
authors: FH
authors: Allain
mesh_terms: D000243:Adenosine Deaminase / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D043542:DNA, Z-Form / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012330:RNA, Double-Stranded / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins
chemical_list: D043542:DNA, Z-Form; D012330:RNA, Double-Stranded; D016601:RNA-Binding Proteins; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase