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Article

Structural role of the conserved cysteines in the dimerization of the viral transmembrane oncoprotein E5.

Biophysical journal - 22 Sept 2010

Windisch Dirk, Hoffmann Silke, Afonin Sergii, Vollmer Stefanie, Benamira Soraya, Langer Birgid, Bürck Jochen, Muhle-Goll Claudia, Ulrich Anne S

Abstract excerpt

The E5 oncoprotein is the major transforming protein of bovine papillomavirus type 1. This 44-residue transmembrane protein can interact with the platelet-derived growth factor receptor β, leading to ligand-independent activation and cell transformation. For productive interaction, E5 needs to dimerize via a C-terminal pair of cysteines, though a recent study suggested that its truncated transmembrane segment can...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 20858420
DOI: 10.1016/j.bpj.2010.06.073
PMCID: PMC2941001

Provenance

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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