Unknown

Dataset Information

0

Crystal structure of the DNA cytosine deaminase APOBEC3F: the catalytically active and HIV-1 Vif-binding domain.


ABSTRACT: Human APOBEC3F is an antiretroviral single-strand DNA cytosine deaminase, susceptible to degradation by the HIV-1 protein Vif. In this study the crystal structure of the HIV Vif binding, catalytically active, C-terminal domain of APOBEC3F (A3F-CTD) was determined. The A3F-CTD shares structural motifs with portions of APOBEC3G-CTD, APOBEC3C, and APOBEC2. Residues identified to be critical for Vif-dependent degradation of APOBEC3F all fit within a predominantly negatively charged contiguous region on the surface of A3F-CTD. Specific sequence motifs, previously shown to play a role in Vif susceptibility and virion encapsidation, are conserved across APOBEC3s and between APOBEC3s and HIV-1 Vif. In this structure these motifs pack against each other at intermolecular interfaces, providing potential insights both into APOBEC3 oligomerization and Vif interactions.

SUBMITTER: Bohn MF 

PROVIDER: S-EPMC3805256 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications


Human APOBEC3F is an antiretroviral single-strand DNA cytosine deaminase, susceptible to degradation by the HIV-1 protein Vif. In this study the crystal structure of the HIV Vif binding, catalytically active, C-terminal domain of APOBEC3F (A3F-CTD) was determined. The A3F-CTD shares structural motifs with portions of APOBEC3G-CTD, APOBEC3C, and APOBEC2. Residues identified to be critical for Vif-dependent degradation of APOBEC3F all fit within a predominantly negatively charged contiguous region  ...[more]

Similar Datasets

| S-EPMC3602375 | biostudies-literature
| S-EPMC4248952 | biostudies-literature
| S-EPMC4956467 | biostudies-literature
| S-EPMC4702671 | biostudies-literature
| S-EPMC4684092 | biostudies-literature
| S-EPMC6899190 | biostudies-literature
| S-EPMC3003379 | biostudies-literature
| S-EPMC3004357 | biostudies-literature
| S-EPMC5142242 | biostudies-literature
| S-EPMC423288 | biostudies-literature