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Identifying long‐range structure in the intrinsically unstructured transactivation domain of p53
Author(s) -
Vise Pamela,
Baral Bharat,
Stancik Amber,
Lowry David F.,
Daughdrill Gary W.
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21364
Subject(s) - transactivation , ubiquitin ligase , mdm2 , suppressor , protein subunit , domain (mathematical analysis) , ubiquitin , intrinsically disordered proteins , p53 protein , computational biology , biology , chemistry , microbiology and biotechnology , biophysics , genetics , transcription factor , mathematics , cancer , gene , mathematical analysis
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.