Nature Communications (Oct 2017)

APOBEC3H structure reveals an unusual mechanism of interaction with duplex RNA

  • Jennifer A. Bohn,
  • Keyur Thummar,
  • Ashley York,
  • Alice Raymond,
  • W. Clay Brown,
  • Paul D. Bieniasz,
  • Theodora Hatziioannou,
  • Janet L. Smith

DOI
https://doi.org/10.1038/s41467-017-01309-6
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 9

Abstract

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The APOBEC3 family cytidine deaminases with antiviral activity are proteins that catalyze the deamination of newly reverse-transcribed viral DNA. Here the authors present the crystal structure of full-length pig-tailed macaque APOBEC3H with bound RNA, which reveals how the APOBEC3H dimer binds around a short RNA duplex.