High-throughput mutagenesis reveals unique structural features of human ADAR1

SeHee Park; Erin E. Doherty; Yixuan Xie; Anil K. Padyana; Fang Fang; Yue Zhang; Agya Karki; Carlito B. Lebrilla; Justin B. Siegel; Peter A. Beal

doi:10.1038/s41467-020-18862-2

Nature Communications (Oct 2020)

High-throughput mutagenesis reveals unique structural features of human ADAR1

SeHee Park,
Erin E. Doherty,
Yixuan Xie,
Anil K. Padyana,
Fang Fang,
Yue Zhang,
Agya Karki,
Carlito B. Lebrilla,
Justin B. Siegel,
Peter A. Beal

Affiliations

SeHee Park: Department of Chemistry, University of California, Davis
Erin E. Doherty: Department of Chemistry, University of California, Davis
Yixuan Xie: Department of Chemistry, University of California, Davis
Anil K. Padyana: Agios Pharmaceuticals
Fang Fang: Viva Biotech Ltd.
Yue Zhang: Department of Chemistry, University of California, Davis
Agya Karki: Department of Chemistry, University of California, Davis
Carlito B. Lebrilla: Department of Chemistry, University of California, Davis
Justin B. Siegel: Department of Chemistry, University of California, Davis
Peter A. Beal: Department of Chemistry, University of California, Davis

DOI: https://doi.org/10.1038/s41467-020-18862-2
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 13

Abstract

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Human ADAR proteins are responsible for RNA editing, conversion of adenosine to inosine in double-stranded RNA. Here the authors report a previously unknown zinc ion-binding site in the catalytic domain of human ADAR1 using high throughput mutagenesis, biochemical assay and Rosetta-based protein structure modeling.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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