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Multifaceted HIV‐1 Vif interactions with human E3 ubiquitin ligase and APOBEC3s
Author(s) -
Hu Yingxia,
Knecht Kirsten M.,
Shen Qi,
Xiong Yong
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15550
Subject(s) - ubiquitin ligase , human immunodeficiency virus (hiv) , ubiquitin , biology , infectivity , apobec3g , virology , ubiquitin protein ligases , host factor , computational biology , viral replication , virus , microbiology and biotechnology , genetics , gene
The recent cryoelectron microscopy structure of the Vif‐targeted domain of human A3F in complex with HIV‐1 Vif and host cofactor CBFβ reveals how the viral protein and cellular cofactor both participate in recruiting A3F to the Cul5 E3 ligase machinery for polyubiquitination and subsequent proteasomal degradation. The novel binding interfaces discovered in the Vif/CBFβ/A3F complex structure could open up new avenues for the development of more effective anti‐HIV therapeutic strategies.