Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
APOBEC3G (A3G) belongs to the DNA/RNA cytosine deaminase family that plays important roles in innate immunity against HIV and internal retroelements. Here the authors report the structures of two full-length A3G variants that provides insight into domain organization, multimerization, RNA binding, a...
Main Authors: | Hanjing Yang, Fumiaki Ito, Aaron D. Wolfe, Shuxing Li, Nazanin Mohammadzadeh, Robin P. Love, Maocai Yan, Brett Zirkle, Amit Gaba, Linda Chelico, Xiaojiang S. Chen |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2020-01-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-14377-y |
Similar Items
-
Special Issue “APOBECs and Virus Restriction”
by: Linda Chelico
Published: (2021-08-01) -
APOBEC3D excludes APOBEC3F from HIV-1 virions by competitive binding of RNA
by: Shreoshri Bhattacharjee, et al.
Published: (2024-01-01) -
Different mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanisms.
by: Anjuman Ara, et al.
Published: (2014-03-01) -
Suppression of APOBEC3-mediated restriction of HIV-1 by Vif
by: Yuqing eFeng, et al.
Published: (2014-08-01) -
Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I
by: Maria Yousefi, et al.
Published: (2023-02-01)