1TBD
SOLUTION STRUCTURE OF THE ORIGIN DNA BINDING DOMAIN OF SV40 T-ANTIGEN, NMR, MINIMIZED AVERAGE STRUCTURE
Summary for 1TBD
| Entry DOI | 10.2210/pdb1tbd/pdb |
| Descriptor | SV40 T-ANTIGEN (1 entity in total) |
| Functional Keywords | dna-binding protein, replication origin binding domain, dna binding protein |
| Biological source | Simian virus 40 |
| Cellular location | Host nucleus: P03070 |
| Total number of polymer chains | 1 |
| Total formula weight | 15414.63 |
| Authors | Luo, X.,Sanford, D.G.,Bullock, P.A.,Bachovchin, W.W. (deposition date: 1996-11-04, release date: 1997-03-12, Last modification date: 2024-05-22) |
| Primary citation | Luo, X.,Sanford, D.G.,Bullock, P.A.,Bachovchin, W.W. Solution structure of the origin DNA-binding domain of SV40 T-antigen. Nat.Struct.Biol., 3:1034-1039, 1996 Cited by PubMed 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 beta-sheet flanked by two alpha-helices on one side and one alpha-helix and one 3(10)-helix on the other, is a new one. Previous mutational analyses have identified two elements, termed A (approximately 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. PubMed: 8946857DOI: 10.1038/nsb1296-1034 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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