1TBD
SOLUTION STRUCTURE OF THE ORIGIN DNA BINDING DOMAIN OF SV40 T-ANTIGEN, NMR, MINIMIZED AVERAGE STRUCTURE
1TBD の概要
| エントリーDOI | 10.2210/pdb1tbd/pdb |
| 分子名称 | SV40 T-ANTIGEN (1 entity in total) |
| 機能のキーワード | dna-binding protein, replication origin binding domain, dna binding protein |
| 由来する生物種 | Simian virus 40 |
| 細胞内の位置 | Host nucleus: P03070 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15414.63 |
| 構造登録者 | Luo, X.,Sanford, D.G.,Bullock, P.A.,Bachovchin, W.W. (登録日: 1996-11-04, 公開日: 1997-03-12, 最終更新日: 2024-05-22) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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