How p53's Structure Affects Its Function
Author Information
Author(s): Natan Eviatar, Baloglu Cetin, Pagel Kevin, Freund Stefan M.V., Morgner Nina, Robinson Carol V., Fersht Alan R., Joerger Andreas C.
Primary Institution: MRC Laboratory of Molecular Biology
Hypothesis
The N-terminal extension of p53 modulates the stability and function of its DNA-binding domain.
Conclusion
The study reveals that the N-terminal extension of p53 enhances the stability of its DNA-binding domain and affects its aggregation properties.
Supporting Evidence
- NMR and X-ray crystallography revealed that Trp91 interacts with Arg174 in the DNA-binding domain.
- The presence of the N-terminal extension increases the melting temperature of the DNA-binding domain.
- The study shows that constructs lacking the N-terminal extension are more prone to aggregation.
Takeaway
This study shows that a small part of the p53 protein helps it stay stable and work properly, which is important for preventing cancer.
Methodology
The study used NMR and X-ray crystallography to investigate the interactions between the N-terminal extension and the DNA-binding domain of p53.
Limitations
The study primarily focuses on specific constructs of p53, which may not fully represent the behavior of the full-length protein in all contexts.
Digital Object Identifier (DOI)
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