Common cancer mutations R175H and R273H drive the p53 DNA-binding domain towards aggregation-prone conformations
Author:
Affiliation:
1. Department of Physics
2. State Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Sciences (Ministry of Education)
3. Multiscale Research Institute of Complex Systems
4. Fudan University
5. Shanghai 200438
Abstract
Cancer mutations R175H and R273H induce p53C towards aggregation-prone conformations by increasing their SASA, water exposure of H-bonds and flexibility of loop2.
Funder
National Natural Science Foundation of China
National Basic Research Program of China
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2020/CP/C9CP06671C
Reference65 articles.
1. Structural Biology of the Tumor Suppressor p53
2. Presence of a Potent Transcription Activating Sequence in the p53 Protein
3. Identification of an additional negative regulatory region for p53 sequence-specific DNA binding
4. Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms
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