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Related Experiment Video

Updated: Nov 4, 2025

Yeast As a Chassis for Developing Functional Assays to Study Human P53

Yeast As a Chassis for Developing Functional Assays to Study Human P53

Published on: August 4, 2019

DNA-Bound p53-DNA-Binding Domain Interconverts between Multiple Conformations: Implications for Partner Protein

Sayan Bhattacharjee¹, Sujoy Mukherjee¹, Siddhartha Roy²

¹Department of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology, 4, Raja S.C. Mullick Road, Kolkata 700032, India.

The Journal of Physical Chemistry. B

|May 27, 2021

Summary

Hub proteins like p53 utilize dynamic conformational changes to interact with diverse partners. DNA binding induces these crucial protein dynamics, enabling p53

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Published on: September 21, 2017

Area of Science:

Molecular biology
Biophysics

Background:

Protein-protein interaction networks are essential for cellular regulation.
Hub proteins, central to these networks, interact with numerous partners.
A hypothesis suggests conformational dynamics enable hub protein interactions.

Purpose of the Study:

To investigate the dynamics of the p53 DNA-binding domain.
To test the hypothesis that conformational flexibility is key to p53's function.

Main Methods:

Utilized 15N-NMR Carr-Purcell-Meiboom-Gill relaxation methods.
Analyzed the dynamics of the p53 DNA-binding domain in both free and DNA-bound states.

Main Results:

Detected microsecond to millisecond timescale conformational exchanges in the DNA-bound p53 domain.
Observed no detectable dynamics at this timescale in the free p53 domain.
Demonstrated that DNA binding promotes conformational exchange in p53.

Conclusions:

DNA binding induces conformational dynamics in the p53 DNA-binding domain.
This dynamic conformational repertoire is crucial for p53's interaction with multiple partners.
Supports the hypothesis that conformational flexibility is vital for hub protein function.