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- W2014126064 abstract "Intrinsically Disordered Proteins (IDPs) are frequently found in vital cellular pathways including transcriptional activation and signal transduction. There is however a dearth of atomic models available for IDPs, hampering insight into how the structural ensemble is specified by the amino acid sequence. Nuclear Overhauser Effect (NOE) data was collected from the intrinsically disordered transactivation domain of a series of p53 (p53TAD) orthologues to investigate the conservation of dynamic behavior. The data suggest the presence of recurring but variable structural elements among the orthologues in the region aligning with the ubiquitin ligase MDM2 binding domain of human p53TAD, and to a lesser extent in the region correlating to the RPA binding domain of human p53TAD. The data also show significant variation in the backbone dynamics at these regions. The recurrence of these structural features across evolutionary time as suggested by the NOE data gives some credence to the idea that transient secondary structures within IDPs are constrained, though with possibly varying degrees of dynamic behavior. Future atomic modeling of the structural ensembles of these homologues should allow for a better understanding of the effect of residue similarity on the final structural ensemble in IDPs." @default.
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- W2014126064 date "2011-02-01" @default.
- W2014126064 modified "2023-09-28" @default.
- W2014126064 title "Evolution of Structure and Dynamics for a Family of Disordered Proteins" @default.
- W2014126064 doi "https://doi.org/10.1016/j.bpj.2010.12.3036" @default.
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