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6SL6

p53 charged core

Summary for 6SL6
Entry DOI10.2210/pdb6sl6/pdb
DescriptorCellular tumor antigen p53, GLYCEROL, ZINC ION, ... (4 entities in total)
Functional Keywordstumor suppressor, aggregation prone, mutant p53, cell cycle
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight28176.15
Authors
Gallardo, R.,Langenberg, T.,Schymkowitz, J.,Rousseau, F.,Ulens, C. (deposition date: 2019-08-18, release date: 2020-03-11, Last modification date: 2024-01-24)
Primary citationLangenberg, T.,Gallardo, R.,van der Kant, R.,Louros, N.,Michiels, E.,Duran-Romana, R.,Houben, B.,Cassio, R.,Wilkinson, H.,Garcia, T.,Ulens, C.,Van Durme, J.,Rousseau, F.,Schymkowitz, J.
Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins.
Cell Rep, 31:107512-107512, 2020
Cited by
PubMed Abstract: The amyloid-like aggregation propensity present in most globular proteins is generally considered to be a secondary side effect resulting from the requirements of protein stability. Here, we demonstrate, however, that mutations in the globular and amyloid state are thermodynamically correlated rather than simply associated. In addition, we show that the standard genetic code couples this structural correlation into a tight evolutionary relationship. We illustrate the extent of this evolutionary entanglement of amyloid propensity and globular protein stability. Suppressing a 600-Ma-conserved amyloidogenic segment in the p53 core domain fold is structurally feasible but requires 7-bp substitutions to concomitantly introduce two aggregation-suppressing and three stabilizing amino acid mutations. We speculate that, rather than being a corollary of protein evolution, it is equally plausible that positive selection for amyloid structure could have been a driver for the emergence of globular protein structure.
PubMed: 32294448
DOI: 10.1016/j.celrep.2020.03.076
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.67 Å)
Structure validation

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