Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-05

AUTHORS

Melissa M Matthews, Justin M Thomas, Yuxuan Zheng, Kiet Tran, Kelly J Phelps, Anna I Scott, Jocelyn Havel, Andrew J Fisher, Peter A Beal

ABSTRACT

Adenosine deaminases acting on RNA (ADARs) are editing enzymes that convert adenosine to inosine in duplex RNA, a modification reaction with wide-ranging consequences in RNA function. Understanding of the ADAR reaction mechanism, the origin of editing-site selectivity, and the effect of mutations is limited by the lack of high-resolution structural data for complexes of ADARs bound to substrate RNAs. Here we describe four crystal structures of the human ADAR2 deaminase domain bound to RNA duplexes bearing a mimic of the deamination reaction intermediate. These structures, together with structure-guided mutagenesis and RNA-modification experiments, explain the basis of the ADAR deaminase domain's dsRNA specificity, its base-flipping mechanism, and its nearest-neighbor preferences. In addition, we identified an ADAR2-specific RNA-binding loop near the enzyme active site, thus rationalizing differences in selectivity observed between different ADARs. Finally, our results provide a structural framework for understanding the effects of ADAR mutations associated with human disease. More... »

PAGES

426-433

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.3203

DOI

http://dx.doi.org/10.1038/nsmb.3203

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017808610

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27065196


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