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Article

Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly.

Journal of virology - 1 Sept 2008

Stanley Bradford J, Ehrlich Elana S, Short Leslie, Yu Yunkai, Xiao Zuoxiang, Yu Xiao-Fang, Xiong Yong

Abstract excerpt

Human immunodeficiency virus (HIV) virion infectivity factor (Vif) causes the proteasome-mediated destruction of human antiviral protein APOBEC3G by tethering it to a cellular E3 ubiquitin ligase composed of ElonginB, ElonginC, Cullin5, and Rbx2. It has been proposed that HIV Vif hijacks the E3 ligase through two regions within its C-terminal domain: a BC box region that interacts with ElonginC and a novel zinc...

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Identifiers

PMID: 18562529
DOI: 10.1128/JVI.00767-08
PMCID: PMC2519636

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly.PMID 18562529Read ↗

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Evolutionarily Conserved Requirement for Core Binding Factor Beta in the Assembly of the Human Immunodeficiency Virus/Simian Immunodeficiency Virus Vif-Cullin 5-RING E3 Ubiquitin LigaseSemantic proximity Read ↗

Structural basis of HIV-1 Vif-mediated E3 ligase targeting of host APOBEC3HSemantic proximity Read ↗

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