ArticleProceedings of the National Academy of Sciences of the United States of America2012
Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 40 citations in OpenAlex.
- How Do Cancer-Related Mutations Affect the Oligomerisation State of the p53 Tetramerisation Domain?Current issues in molecular biology · 2023Article
- Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR.Biochemistry · 2022Article
- Structural Basis of Mutation-Dependent p53 Tetramerization Deficiency.International journal of molecular sciences · 2022Article
- A phosphorylation-dependent switch in the disordered p53 transactivation domain regulates DNA binding.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Investigating Conformational Dynamics and Allostery in the p53 DNA-Binding Domain Using Molecular Simulations.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Interaction between p53 N terminus and core domain regulates specific and nonspecific DNA binding.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Characterization of an Hsp90-Independent Interaction between Co-Chaperone p23 and Transcription Factor p53.Biochemistry · 2018Article
- Structures of closed and open conformations of dimeric human ATM.Science advances · 2017Article
- DNA-binding protects p53 from interactions with cofactors involved in transcription-independent functions.Nucleic acids research · 2016Article
- Multi-scale ensemble modeling of modular proteins with intrinsically disordered linker regions: application to p53.Biophysical journal · 2014Article
- Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases.Chemical reviews · 2014Review
- Characterizing functional domains for TIM-mediated enveloped virus entry.Journal of virology · 2014Article
- CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions.Journal of biomolecular NMR · 2014Article
- MDMX contains an autoinhibitory sequence element.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Molecular dynamics of the full-length p53 monomer.Cell cycle (Georgetown, Tex.) · 2013Article
- The quiet renaissance of protein nuclear magnetic resonance.Biochemistry · 2013Review
- Mapping the structural and dynamical features of multiple p53 DNA binding domains: insights into loop 1 intrinsic dynamics.PloS one · 2013Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The tumor suppressor p53 is a homotetramer of 4 × 393 residues. Its core domain and tetramerization domain are linked and flanked by intrinsically disordered sequences, which hinder its full structural characterization. There is an outstanding problem of the state of the tetramerization domain. Structural studies on the isolated tetramerization domain show it is in a folded tetrameric conformation, but there are conflicting models from electron microscopy of the full-length protein, one of which proposes that the domain is not tetramerically folded and the tetrameric protein is stabilized by interactions between the N and C termini. Here, we present methyl-transverse relaxation optimized NMR spectroscopy (methyl-TROSY) investigations on the full-length and separate domains of the protein with its methionine residues enriched with (13)C to probe its quaternary structure. We obtained high-quality spectra of both the full-length tetrameric p53 and its DNA complex, observing the environment at 11 specific methyl sites. The tetramerization domain was as tetramerically folded in the full-length constructs as in the isolated domain. The N and C termini were intrinsically disordered in both the full-length protein and its complex with a 20-residue specific DNA sequence. Additionally, we detected in the interface of the core (DNA-binding) and N-terminal parts of the protein a slow conformational exchange process that was modulated by specific recognition of DNA, indicating allosteric processes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.