Abstract
The structure of the domain from simian virus 40 (SV40) large T-antigen that binds to the SV40 origin of DNA replication (T-ag-OBD131–260) has been determined by nuclear magnetic resonance spectroscopy. The overall fold, consisting of a central five-stranded antiparallel β-sheet flanked by two α-helices on one side and one α-helix and one 310-helix on the other, is a new one. Previous mutational analyses have identified two elements, termed A (∼152–155) and B2 (203–207), as essential for origin-specific recognition. These elements form two closely juxtaposed loops that define a continuous surface on the protein. The addition of a duplex oligonucleotide containing the origin recognition pentanucleotide GAGGC induces chemical shift changes and slows amide proton exchange in resonances from this region, indicating that this surface directly contacts the DNA.
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Luo, X., Sanford, D., Bullock, P. et al. Solution structure of the origin DNA-binding domain of SV40 T-antigen. Nat Struct Mol Biol 3, 1034–1039 (1996). https://doi.org/10.1038/nsb1296-1034
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DOI: https://doi.org/10.1038/nsb1296-1034
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