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Article

Functional and Structural Insights into a Vif/PPP2R5 Complex Elucidated Using Patient HIV-1 Isolates and Computational Modeling.

Journal of virology - 14 Oct 2020

Salamango Daniel J, McCann Jennifer L, Demir Özlem, Becker Jordan T, Wang Jiayi, Lingappa Jairam R, Temiz Nuri A, Brown William L, Amaro Rommie E, Harris Reuben S

Abstract excerpt

Human immunodeficiency virus type 1 (HIV-1) Vif recruits a cellular ubiquitin ligase complex to degrade antiviral APOBEC3 enzymes (APOBEC3C-H) and PP2A phosphatase regulators (PPP2R5A to PPP2R5E). While APOBEC3 antagonism is the canonical function of HIV-1 Vif, this viral accessory protein is also known to trigger G2/M cell cycle arrest. Vif initiates G2/M arrest by degrading multiple PPP2R5 family members, an...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Interaction Domains and Motifs

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Share to vif Gene Products, Human Immunodeficiency Virus

Source

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Identifiers

PMID: 32847850
DOI: 10.1128/JVI.00631-20
PMCID: PMC7565612

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Functional and Structural Insights into a Vif/PPP2R5 Complex Elucidated Using Patient HIV-1 Isolates and Computational Modeling.PMID 32847850Read ↗

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