Model structure of APOBEC3C reveals a binding pocket modulating ribonucleic acid interaction required for encapsidation.

ABSTRACT: Human APOBEC3 (A3) proteins form part of the intrinsic immunity to retroviruses. Carrying 1 or 2 copies of a cytidine deaminase motif, A3s act by deamination of retroviral genomes during reverse transcription. HIV-1 overcomes this inhibition by the Vif protein, which prevents incorporation of A3 into virions. In this study we modeled and probed the structure of APOBEC3C (A3C), a single-domain A3 with strong antilentiviral activity. The 3-dimensional protein model was used to predict the effect of mutations on antiviral activity, which was tested in a Deltavif simian immunodeficiency virus (SIV) reporter virus assay. We found that A3C activity requires protein dimerization for antiviral activity against SIV. Furthermore, by using a structure-based algorithm for automated pocket extraction,

SUBMITTER: Stauch B 

PROVIDER: S-EPMC2715496 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature