ArticleJournal of virology2011
Structure-based analysis of the interaction between the simian virus 40 T-antigen origin binding domain and single-stranded DNA.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- Insights into the A-C Mismatch Conformational Ensemble in Duplex DNA and its Role in Genetic Processes through a Structure-based Review.Journal of molecular biology · 2024Review
- SV40 T antigen interactions with ssDNA and replication protein A: a regulatory role of T antigen monomers in lagging strand DNA replication.Nucleic acids research · 2020Article
- Article
- Insights into the initiation of JC virus DNA replication derived from the crystal structure of the T-antigen origin binding domain.PLoS pathogens · 2014Article
- Analysis of the costructure of the simian virus 40 T-antigen origin binding domain with site I reveals a correlation between GAGGC spacing and spiral assembly.Journal of virology · 2013Article
- Modeling of the SV40 DNA Replication Machine.Genes · 2012Article
- Asymmetric assembly of Merkel cell polyomavirus large T-antigen origin binding domains at the viral origin.Journal of molecular biology · 2011Article
- Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain.Acta crystallographica. Section D, Biological crystallography · 2011Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The origin-binding domain (OBD) of simian virus 40 (SV40) large T-antigen (T-Ag) is essential for many of T-Ag's interactions with DNA. Nevertheless, many important issues related to DNA binding, for example, how single-stranded DNA (ssDNA) transits along the T-Ag OBD, have yet to be established. Therefore, X-ray crystallography was used to determine the costructure of the T-Ag OBD bound to DNA substrates such as the single-stranded region of a forked oligonucleotide. A second structure of the T-Ag OBD crystallized in the presence of poly(dT)(12) is also reported. To test the conclusions derived from these structures, residues identified as being involved in binding to ssDNA by crystallography or by an earlier nuclear magnetic resonance study were mutated, and their binding to DNA was characterized via fluorescence anisotropy. In addition, these mutations were introduced into full-length T-Ag, and these mutants were tested for their ability to support replication. When considered in terms of additional homology-based sequence alignments, our studies refine our understanding of how the T-Ag OBDs encoded by the polyomavirus family interact with ssDNA, a critical step during the initiation of DNA replication.
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