The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure
Open accessAbstract
Brca1 C-terminal (BRCT) domains are a common protein–protein interaction motif in proteins involved in the DNA damage response and DNA repair. The DNA-damage response protein 53BP1 has two BRCT domains that bind to the DNA-binding domain of p53. The 53BP1 tandem-BRCT region is homologous to the tandem-BRCT region of Brca1, which is involved in double-strand break repair and homologous recombination and which binds BACH1, a member of the DEAH helicase family. Here we report the structures of a human 53BP1–p53 complex and of the rat Brca1 BRCT repeats. The 53BP1–p53 structure shows that the two BRCT repeats are arranged tandemly and pack extensively through an interface that also involves the inter-repeat linker. The first BRCT repeat and the linker together bind p53 on a region that overlaps with the DNA-binding surface of p53 and involves p53 residues that are mutated in cancer and are important for DNA binding. Comparison with the structure of the tandem-BRCT region of Brca1 shows a remarkable conservation of the repeat arrangement and of the inter-BRCT repeat interface. Analysis of human BRCA1 tumor-derived mutations and conservation identifies a potential protein-binding site that we show through mutagenesis is involved in BACH1 binding. The BACH1-binding region of Brca1 consists of a unique insertion in the first BRCT repeat and the inter-repeat linker and is analogous to the region of 53BP1 that binds p53.
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Citations
Cites
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
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“The L3 loop is one of the two key structural elements that make up the DNA-binding surface of p53, containing an arginine residue (Arg 248) that binds in the minor groove of the DNA (Cho et al. 1994).”
BackgroundMethodInfluentialSelf-citationBrca1 Controls Homology-Directed DNA Repair
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“…disperse and redistribute to new foci that contain Rad51, which is the mammalian homolog of the Escherichia coli RecA protein that mediates DNA recombination, PCNA (Scully et al. 1997) and the Rad50/ Mre11/NBS1 complex (Zhong et al. 1999; Wang et al. 2000; Wu et al. 2000; Chiba and Parvin 2001).”
BackgroundA superfamily of conserved domains in DNA damage‐ responsive cell cycle checkpoint proteins
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Self-citation
Cited by
Acetylation Is Indispensable for p53 Activation
Tang, Y., Zhao, W., Chen, Y., Zhao, Y., & Gu, W. (2008) · Cell · doi:10.1016/j.cell.2008.03.025 · Cited by 838
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
53BP1, a Mediator of the DNA Damage Checkpoint
Wang, B., Matsuoka, S., Carpenter, P. B., & Elledge, S. J. (2002) · Science · doi:10.1126/science.1076182 · Cited by 578
Structural Basis of DNA Recognition by p53 Tetramers
Kitayner, M., Rozenberg, H., Kessler, N., Rabinovich, D., Shaulov, L., Haran, T. E., & Shakked, Z. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.015 · Cited by 408
Thompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357
Metadata
- Authors
- Joo, W. S., Jeffrey, P. D., Cantor, S. B., Finnin, M. S., Livingston, D. M., & Pavletich, N. P.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2002-03-01
- Volume
- 16
- Issue
- 5
- Pages
- 583-593
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2140970553
- Cited by
- 220
- References
- 5
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Joo, W. S., Jeffrey, P. D., Cantor, S. B., Finnin, M. S., Livingston, D. M., & Pavletich, N. P. (2002). Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure. Genes & Development. https://doi.org/10.1101/gad.959202
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