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Crystal structure of SV40 large T-antigen bound to p53: interplay between a viral oncoprotein and a cellular tumor suppressor
Abstract
The transformation potential of Simian Virus 40 depends on the activities of large T-antigen (LTag), which interacts with several cellular tumor suppressors including the important “guardian” of the genome, p53. Inhibition of p53 function by LTag is necessary for both efficient viral replication and cellular transformation. We determined the crystal structure of LTag in complex with p53. The structure reveals an unexpected hexameric complex of LTag binding six p53 monomers. Structure-guided mutagenesis of LTag and p53 residues supported the p53–LTag interface defined by the complex structure. The structure also shows that LTag binding induces dramatic conformational changes at the DNA-binding area of p53, which is achieved partially through an unusual “methionine switch” within p53. In the complex structure, LTag occupies the whole p53 DNA-binding surface and likely interferes with formation of a functional p53 tetramer. In addition, we showed that p53 inhibited LTag helicase function through direct complex formation.
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“LTag promotes viral replication and cellular transformation.”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [310]
In the citing paper
“The p53-DBD is also targeted by viral oncoproteins, such as the large T antigen (LTag) of simian virus 40 (SV40)310 (Fig. 7h) and human papillomavirus (HPV) oncoprotein E6311,312 (Fig. 7i).”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [310]
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“It occupies the entire DNA-binding surface of p53-DBD and interacts with a region of helix H1 that is involved in p53-DBD dimerization.”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [310]
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Citations
Cites
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Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
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“In the crystal structure of the p53–DNA complex, the L3 loop of p53 makes several important contacts with DNA (Cho et al. 1994).”
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Cited by
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016
(2024) · doi:10.1128/msphere.00799-23 · Cited by 23
Metadata
- Authors
- Lilyestrom, W., Klein, M. G., Zhang, R., Joachimiak, A., & Chen, X. S.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2006-09-01
- Volume
- 20
- Issue
- 17
- Pages
- 2373-2382
- ISSN
- 0890-9369
- 1549-5477
- Cited by
- 132
- References
- 5
- Language
- en
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