The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2
Abstract
Mutations in the p53 tumor suppressor are among the most frequently observed genetic alterations in human cancer and map to the 200-amino acid core domain of the protein. The core domain contains the sequence-specific DNA binding activity and the in vitro 53BP2 protein binding activity of p53. The crystal structure of the p53 core domain bound to the 53BP2 protein, which contains an SH3 (Src homology 3) domain and four ankyrin repeats, revealed that (i) the SH3 domain binds the L3 loop of p53 in a manner distinct from that of previously characterized SH3-polyproline peptide complexes, and (ii) an ankyrin repeat, which forms an L-shaped structure consisting of a β hairpin and two α helices, binds the L2 loop of p53. The structure of the complex shows that the 53BP2 binding site on the p53 core domain consists of evolutionarily conserved regions that are frequently mutated in cancer and that it overlaps the site of DNA binding. The six most frequently observed p53 mutations disrupt 53BP2 binding in vitro. The structure provides evidence that the 53BP2-p53 complex forms in vivo and may have a critical role in the p53 pathway of tumor suppression.
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“They interact with p53-DBD through the L3 loop and L2 loop304–306 (Fig. 7c, e).”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [305]
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Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
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Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
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Self-citationMice Lacking p21CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control
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Cited by
The Cell–Cycle Arrest and Apoptotic Functions of p53 in Tumor Initiation and Progression
Chen, J. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026104 · Cited by 1,222
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 p16INK4a/CDKN2A tumor suppressor and its relatives
Ruas, M., & Peters, G. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(98)00017-1 · Cited by 911
ASPP Proteins Specifically Stimulate the Apoptotic Function of p53
Samuels-Lev, Y., O'Connor, D. J., Bergamaschi, D., Trigiante, G., Hsieh, J.-K., Zhong, S., Campargue, I., Naumovski, L., Crook, T., & Lu, X. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00367-7 · Cited by 664
Binz, H. K., Stumpp, M. T., Forrer, P., Amstutz, P., & Plückthun, A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00896-9 · Cited by 589
Metadata
- Authors
- Gorina, S., & Pavletich, N. P.
- Venue
- Science
- Published
- 1996-11-08
- Volume
- 274
- Issue
- 5289
- Pages
- 1001-1005
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2089623038
- Cited by
- 571
- References
- 10
- FWCI
- 17.25
- Type
- journal article
- Language
- en
- Open access
- closed
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- Gorina, S., & Pavletich, N. P. (1996). Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2. Science. https://doi.org/10.1126/science.274.5289.1001
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