Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 67, Issue 3, Pages 526-530Publisher
WILEY
DOI: 10.1002/prot.21364
Keywords
ensemble; distance; paramagnetic; relaxation; enhancement
Categories
Funding
- NCRR NIH HHS [P20 RR 16448, P20 RR 16454-02] Funding Source: Medline
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Paramagnetic relaxation enhancement (PRE) was used to identify a compact dynamic structure for the intrinsically unstructured transactivation domain of the tumor suppressor protein, p53. Our results show that p53 residues essential for binding to the ubiquitin ligase, MDM2, and the 70 kDa subunit of replication protein A, RPA70, are separated by an average distance of 10-15 angstrom. This result suggests that a more extended member of the ensemble must be populated prior to binding either MDM2 or RPA70. We also show that PRE can be used to detect intermolecular distances between p53 and RPA70.
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