ArticleProceedings of the National Academy of Sciences of the United States of America2017
Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Recent advances in human papillomavirus vaccines and therapeutic strategies: Combating cervical and non-cervical cancers.Genes & diseases · 2026Review
- Article
- Digital droplet PCR-based detection and quantification of ovine papillomavirus DNA from the vaginal virobiota of healthy mares.Scientific reports · 2025Article
- Molecular findings and virological assessment of bladder papillomavirus infection in cattle.The veterinary quarterly · 2024Article
- De novo-designed transmembrane proteins bind and regulate a cytokine receptor.Nature chemical biology · 2024Article
- Vertical Intrauterine Bovine and Ovine Papillomavirus Coinfection in Pregnant Cows.Pathogens (Basel, Switzerland) · 2024Article
- Article
- Molecular Detection and Quantification of Ovine Papillomavirus DNA in Equine Sarcoid.Transboundary and emerging diseases · 2024Article
- Possible etiological association of ovine papillomaviruses with bladder tumors in cattle.Virus research · 2023Review
- On a mechanistic impact of transmembrane tetramerization in the pathological activation of RTKs.Computational and structural biotechnology journal · 2023Article
- Discovering immunoreceptor coupling and organization motifs.Frontiers in immunology · 2023Article
- Metatranscriptomics Analysis Reveals Diverse Viral RNA in Cutaneous Papillomatous Lesions of Cattle.Evolutionary bioinformatics online · 2022Article
- Activation of the PDGF β Receptor by a Persistent Artificial Signal Peptide.Journal of molecular biology · 2021Article
- Conformational Clamping by a Membrane Ligand Activates the EphA2 Receptor.Journal of molecular biology · 2021Article
- The human papillomavirus oncoproteins: a review of the host pathways targeted on the road to transformation.The Journal of general virology · 2021Review
- Review
- Association Between BoLA-DRB3.2 Polymorphism and Bovine Papillomavirus Infection for Bladder Tumor Risk in Podolica Cattle.Frontiers in veterinary science · 2021Article
- Bovine Papillomavirus Type 2 Infection Associated with Papillomatosis of the Amniotic Membrane in Water Buffaloes (Pathogens (Basel, Switzerland) · 2020Article
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Biologically Active Ultra-Simple Proteins Reveal Principles of Transmembrane Domain Interactions.Journal of molecular biology · 2019Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
The dimeric 44-residue E5 protein of bovine papillomavirus is the smallest known naturally occurring oncoprotein. This transmembrane protein binds to the transmembrane domain (TMD) of the platelet-derived growth factor β receptor (PDGFβR), causing dimerization and activation of the receptor. Here, we use Rosetta membrane modeling and all-atom molecular dynamics simulations in a membrane environment to develop a chemically detailed model of the E5 protein/PDGFβR complex. In this model, an active dimer of the PDGFβR TMD is sandwiched between two dimers of the E5 protein. Biochemical experiments showed that the major PDGFβR TMD complex in mouse cells contains two E5 dimers and that binding the PDGFβR TMD to the E5 protein is necessary and sufficient to recruit both E5 dimers into the complex. These results demonstrate how E5 binding induces receptor dimerization and define a molecular mechanism of receptor activation based on specific interactions between TMDs.
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