期刊
FEBS LETTERS
卷 583, 期 3, 页码 556-560出版社
WILEY
DOI: 10.1016/j.febslet.2008.12.060
关键词
Intrinsically disordered protein; p53 transactivation domain; Protein folding; Molecular dynamics simulation; Leucine-rich hydrophobic cluster
资金
- Barcelona Supercomputing Center
- CONACYT
Molecular dynamics simulations have been performed on the intrinsically disordered 39-residue N-terminal transactivation domain of p53 (p53(1-39)). Simulations not only revealed that p53(1-39) is natively compact, but also possesses a folded structure. Furthermore, leucine-rich hydrophobic clusters were found to play a crucial role in the formation and stabilization of the folded structure of p53(1-39). Collapsing in the sub-microsecond timescale might allow for rapid conformational turnovers of p53(1-39), necessary for its efficient transactivation activity and modulation. Fast collapsing might be the result of unique conformational landscapes, featuring several energy minima separated by small energy barriers. It is suggested that IDPs with highly specialized functions in the cell, such as transactivation, possibly display more ordered patterns than their less specialized counterparts. (c) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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