The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex
Abstract
The homotetrameric tumor suppressor p53 consists of folded core and tetramerization domains, linked and flanked by intrinsically disordered segments that impede structure analysis by x-ray crystallography and NMR. Here, we solved the quaternary structure of human p53 in solution by a combination of small-angle x-ray scattering, which defined its shape, and NMR, which identified the core domain interfaces and showed that the folded domains had the same structure in the intact protein as in fragments. We combined the solution data with electron microscopy on immobilized samples that provided medium resolution 3D maps. Ab initio and rigid body modeling of scattering data revealed an elongated cross-shaped structure with a pair of loosely coupled core domain dimers at the ends, which are accessible for binding to DNA and partner proteins. The core domains in that open conformation closed around a specific DNA response element to form a compact complex whose structure was independently determined by electron microscopy. The structure of the DNA complex is consistent with that of the complex of four separate core domains and response element fragments solved by x-ray crystallography and contacts identified by NMR. Electron microscopy on the conformationally mobile, unbound p53 selected a minor compact conformation, which resembled the closed conformation, from the ensemble of predominantly open conformations. A multipronged structural approach could be generally useful for the structural characterization of the rapidly growing number of multidomain proteins with intrinsically disordered regions.
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“Four Taz2 domains bind to the four N-terminal TADs that were shown to be extended and flexible in unbound tetrameric p53 (5).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [5]
In the citing paper
“The structure of the p53(96–360) construct (comprising the core domain, linker, and tetramerization domains) in complex with DNA, determined by EM and SAXS (5) was used as the starting point of this model.”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [5]
In the citing paper
“A combination of NMR, electron microscopy, small-angle X-ray scattering, and FRET techniques indicates that the free p53 tetramer in solution forms an open cross-shaped structure with a pair of loosely coupled DBD.323,324”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [324]
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“The oligomers close to form a compact complex upon binding a specific DNA response element.”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [324]
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Cited by
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
Putnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184
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
The expanding universe of p53 targets
Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
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Metadata
- Authors
- Tidow, H., Melero, R., Mylonas, E., Freund, S. M. V., Grossmann, J. G., Carazo, J. M., Svergun, D. I., Valle, M., & Fersht, A. R.
- Affiliations
- *Medical Research Council Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom;
- Centro Nacional de Biotecnología, Darwin 3, Cantoblanco 28049 Madrid, Spain;
- European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 Hamburg, Germany;
- Molecular Biophysics Group, Council for the Central Laboratory of the Research Councils (CCLRC) Daresbury Laboratory, Warrington, Cheshire WA4 4AD, United Kingdom
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-07-24
- Volume
- 104
- Issue
- 30
- Pages
- 12324-12329
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 170
- References
- 10
- Language
- en
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