Journal article
Identifying long-range structure in the intrinsically unstructured transactivation domain of p53
Proteins, structure, function, and bioinformatics, Vol.67(3), pp.526-530
05/15/2007
Handle:
https://hdl.handle.net/2376/108818
PMID: 17335006
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.
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Details
- Title
- Identifying long-range structure in the intrinsically unstructured transactivation domain of p53
- Creators
- Pamela Vise - Department of Microbiology, Molecular Biology, and Biochemistry, University of Idaho, Moscow, Idaho 83844-3052, USABharat BaralAmber StancikDavid F LowryGary W Daughdrill
- Publication Details
- Proteins, structure, function, and bioinformatics, Vol.67(3), pp.526-530
- Academic Unit
- Engineering and Applied Sciences (TRIC), School of
- Publisher
- United States
- Grant note
- P20 RR 16448 / NCRR NIH HHS P20 RR 16454-02 / NCRR NIH HHS
- Identifiers
- 99900547384001842
- Language
- English
- Resource Type
- Journal article