Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Espinoza-Fonseca LMdoi
10.1016/j.febslet.2008.12.060subject
Has Abstractpub_date
2009-02-04 00:00:00pages
556-60issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00017-9journal_volume
583pub_type
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