NMR-based structural characterization of large protein-ligand interactions

被引:0
作者
Maurizio Pellecchia
David Meininger
Qing Dong
Edcon Chang
Rick Jack
Daniel S. Sem
机构
[1] Triad Therapeutics,
[2] Inc,undefined
来源
Journal of Biomolecular NMR | 2002年 / 22卷
关键词
drug design; drug discovery; ligand binding; ligand docking; NMR; protein structure;
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暂无
中图分类号
学科分类号
摘要
Genomic research on target identification and validation has created a great need for methods that rapidly provide detailed structural information on protein-ligand interactions. We developed a suite of NMR experiments as rapid and efficient tools to provide descriptive structural information on protein-ligand complexes. The methods work with large proteins and in particular cases also without the need for a complete three-dimensional structure. We will show applications with two tetrameric enzymes of 120 and 170 kDa.
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页码:165 / 173
页数:8
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共 103 条
[1]  
Anil-Kumar R.R.(1980)undefined Biochem. Biophys. Res. Comm. 95 1-6
[2]  
Ernst K.(1995)undefined J. Biol. NMR 6 1-10
[3]  
Wüthrich C.(1990)undefined J. Magn Reson. 86 304-318
[4]  
Bartels T.(2000)undefined J. Biomol. NMR 18 65-68
[5]  
Xia M.(1996)undefined J. Med. Chem. 39 1872-1884
[6]  
Billeter P.(1984)undefined Proc. Natl. Acad. Sci. USA 81 3998-4002
[7]  
Güntert K.(1965)undefined J. Biol. Chem. 240 4717-4722
[8]  
Wüthrich A.(1988)undefined J. Magn. Reson. 78 588-593
[9]  
Bax M.(1991)undefined J. Magn. Reson. 93 93-141
[10]  
Ikura L.E.(2000)undefined Curr. Opin. Struct. Biol. 10 585-592