Cited by 202HIV Research and TreatmentUbiquitin and proteasome pathwaysEnzyme Structure and Function

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Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif

Guo, Yingying, Dong, Liyong, Qiu, Xiaolin, Wang, Yishu, Zhang, Bailing, Liu, Hongnan, Yu, You, Zang, Yi, Yang, Maojun, Huang, Zhiwei·2014·Nature

DOI 10.1038/nature12884

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Abstract

The human immunodeficiency virus (HIV)-1 protein Vif has a central role in the neutralization of host innate defences by hijacking cellular proteasomal degradation pathways to subvert the antiviral activity of host restriction factors; however, the underlying mechanism by which Vif achieves this remains unclear. Here we report a crystal structure of the Vif-CBF-β-CUL5-ELOB-ELOC complex. The structure reveals that Vif, by means of two domains, organizes formation of the pentameric complex by interacting with CBF-β, CUL5 and ELOC. The larger domain (α/β domain) of Vif binds to the same side of CBF-β as RUNX1, indicating that Vif and RUNX1 are exclusive for CBF-β binding. Interactions of the smaller domain (α-domain) of Vif with ELOC and CUL5 are cooperative and mimic those of SOCS2 with the latter two proteins. A unique zinc-finger motif of Vif, which is located between the two Vif domains, makes no contacts with the other proteins but stabilizes the conformation of the α-domain, which may be important for Vif-CUL5 interaction. Together, our data reveal the structural basis for Vif hijacking of the CBF-β and CUL5 E3 ligase complex, laying a foundation for rational design of novel anti-HIV drugs.

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Authors: Guo, Y., Dong, L., Qiu, X., Wang, Y., Zhang, B., Liu, H., Yu, Y., Zang, Y., Yang, M., & Huang, Z.
Affiliations: Harbin Institute of Technology (CN)
Center for Life Sciences (CN)
Corresponding author: Huang, Zhiwei
ORCID: Guo, Yingying
Wang, Yishu
Zhang, Bailing
Yu, You
Yang, Maojun
Huang, Zhiwei
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2014-01
Volume: 505
Issue: 7482
Pages: 229-233
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature12884
OpenAlex: W2049689155
Cited by: 202
References: 36
Citations by year: 2026: 8 · 2025: 4 · 2024: 7 · 2023: 9 · 2022: 14 · 2021: 18 · 2020: 18 · 2019: 14 · 2018: 13 · 2017: 21 · 2016: 18 · 2015: 30 · 2014: 28
FWCI: 14.42
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: HIV-1 Vif, CBFβ, CUL5, elongin B, ELOC, E3 ubiquitin ligase, host restriction factors, proteasomal degradation, zinc finger, RUNX1, crystal structure, antiviral drug targets, HIV-1 replication, protein-protein interaction
MeSH terms: Elongin, Amino Acid Sequence, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Transcription Factors, Protein Structure, Tertiary, Crystallography, X-Ray, Cullin Proteins, Multiprotein Complexes, Core Binding Factor beta Subunit, Core Binding Factor Alpha 2 Subunit, Suppressor of Cytokine Signaling Proteins, vif Gene Products, Human Immunodeficiency Virus, Protein Stability

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Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif

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