title: Identifying long-range structure in the intrinsically unstructured transactivation domain of p53.
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 A. 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.
authors.affiliation: Department of Microbiology, Molecular Biology, and Biochemistry, University of Idaho, Moscow, Idaho 83844-3052, USA.
authors.forename: Pamela
authors.initials: P
authors.lastname: Vise
authors.forename: Bharat
authors.initials: B
authors.lastname: Baral
authors.forename: Amber
authors.initials: A
authors.lastname: Stancik
authors.forename: David F
authors.initials: DF
authors.lastname: Lowry
authors.forename: Gary W
authors.initials: GW
authors.lastname: Daughdrill
mesh_terms: D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D051736:Proto-Oncogene Proteins c-mdm2 / Q000737:chemistry* / Q000378:metabolism; D051716:Replication Protein A / Q000737:chemistry* / Q000378:metabolism; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000378:metabolism
chemical_list: D051716:Replication Protein A; D016159:Tumor Suppressor Protein p53; D051736:Proto-Oncogene Proteins c-mdm2