Summary
PDB 2H1L deposited: 2006-05-16 modified: 2009-02-24
Title The Structure of the Oncoprotein SV40 Large T Antigen and p53 Tumor Suppressor Complex
Authors Chen, X.S., Joachimiak, A., Klein, M.G., Lilyestrom, W., Zhang, R.
Method X-RAY DIFFRACTION
Structure factors resolution 3.16 rfactor 0.2614 rfree 0.3081
DPI 1.08 theoretical min: 0.78
Citations

"The transformation potential of Simian Virus 40 depends on the activities of large T-antigen (LTag), which interacts with several cellular tumor suppressors including the important ""guardian"" of the genome, p53. Inhibition of p53 function by LTag is necessary for both efficient viral replication and cellular transformation. We determined the crystal structure of LTag in complex with p53. The structure reveals an unexpected hexameric complex of LTag binding six p53 monomers. Structure-guided mutagenesis of LTag and p53 residues supported the p53-LTag interface defined by the complex structure. The structure also shows that LTag binding induces dramatic conformational changes at the DNA-binding area of p53, which is achieved partially through an unusual ""methionine switch"" within p53. In the complex structure, LTag occupies the whole p53 DNA-binding surface and likely interferes with formation of a functional p53 tetramer. In addition, we showed that p53 inhibited LTag helicase function through direct complex formation."

Genes Dev. 2006 Sep; 20(17):2373-2382 doi:10.1101/gad.1456306

Cross References
Database source Identifier Description
PubMed 16951253 GEDEEP
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
2H1L/1 2H1L 1 dodecamer 0 12 12 24008
2H1L/2 2H1L 2 dodecamer 0 12 12 23994