Solution structure of the origin DNA-binding domain of SV40 T-antigen

被引：98

作者：

Luo, XL ^{[1
]}

Sanford, DG ^{[1
]}

Bullock, PA ^{[1
]}

Bachovchin, WW ^{[1
]}

机构：

[1] TUFTS UNIV,SCH MED,DEPT BIOCHEM,BOSTON,MA 02111

来源：

NATURE STRUCTURAL BIOLOGY | 1996年 / 3卷 / 12期

关键词：

D O I：

10.1038/nsb1296-1034

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 (similar to 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.

引用

页码：1034 / 1039

页数：6

共 31 条

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