Simulations of mutant p53 DNA binding domains reveal a novel druggable pocket
The DNA binding domain (DBD) of the tumor suppressor p53 is the site of several oncogenic mutations. A subset of these mutations lowers the unfolding temperature of the DBD. Unfolding leads to the exposure of a hydrophobic β-strand and nucleates aggregation which results in pathologies through loss...
Main Authors: | Siau, Jia Wei, Kannan, Srinivasaraghavan, Ouaray, Zohra, Kwoh, Chee Keong, Ghadessy, Farid, Pradhan, Mohan Rajan, Nguyen, Minh N., Lane, David P., Verma, Chandra Shekhar |
---|---|
Other Authors: | School of Computer Science and Engineering |
Format: | Journal Article |
Language: | English |
Published: |
2019
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/105824 http://hdl.handle.net/10220/48748 |
Similar Items
-
Domain-specific p53 mutants activate EGFR by distinct mechanisms exposing tissue-independent therapeutic vulnerabilities
by: Ho, Teresa Lai Fong, et al.
Published: (2023) -
Long range recognition and selection in IDPs : the interactions of the C-terminus of p53
by: Kannan, Srinivasaraghavan, et al.
Published: (2018) -
Roles of computational modelling in understanding p53 structure, biology, and its therapeutic targeting
by: Tan, Yaw Sing, et al.
Published: (2019) -
Pyrimidine Triones as Potential Activators of p53 Mutants
by: Maryam M. Jebril Fallatah, et al.
Published: (2024-08-01) -
The dual interactions of p53 with MDM2 and p300 : implications for the design of MDM2 inhibitors
by: Kannan, Srinivasaraghavan, et al.
Published: (2020)