Identifying Long-range Structure in the Intrinsically Unstructured Transactivation Domain of P53
Document Type
Article
Publication Date
2007
Digital Object Identifier (DOI)
https://doi.org/10.1002/prot.21364
Abstract
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 Å. 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. Proteins 2007. © 2007 Wiley-Liss, Inc.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Proteins: Structure, Function, and Bioinformatics, v. 67, issue 3, p. 526-530
Scholar Commons Citation
Vise, Pamela D.; Baral, Bharat; Stancik, Amber; Lowry, David F.; and Daughdrill, Gary W., "Identifying Long-range Structure in the Intrinsically Unstructured Transactivation Domain of P53" (2007). Molecular Biosciences Faculty Publications. 155.
https://digitalcommons.usf.edu/bcm_facpub/155
