ADAR proteins: Structure and catalytic mechanism

Rena A. Goodman, Mark R. MacBeth, Peter A. Beal

Research output: Chapter in Book/Report/Conference proceedingChapter

42 Scopus citations

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 USA 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.

Original languageEnglish (US)
Title of host publicationCurrent Topics in Microbiology and Immunology
Pages1-33
Number of pages33
Volume353
Edition1
DOIs
StatePublished - 2012

Publication series

NameCurrent Topics in Microbiology and Immunology
Number1
Volume353
ISSN (Print)0070217X

ASJC Scopus subject areas

  • Immunology and Allergy
  • Microbiology (medical)
  • Immunology
  • Microbiology

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