NMR-based structural characterization of large protein-ligand interactions

被引：91

作者：

Pellecchia, M ^{[1
]}

Meininger, D ^{[1
]}

Dong, Q ^{[1
]}

Chang, E ^{[1
]}

Jack, R ^{[1
]}

Sem, DS ^{[1
]}

机构：

[1] Triad Therapeut Inc, San Diego, CA 92121 USA

来源：

JOURNAL OF BIOMOLECULAR NMR | 2002年 / 22卷 / 02期

关键词：

drug design; drug discovery; ligand binding; ligand docking; NMR; protein structure;

D O I：

10.1023/A:1014256707875

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：

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.

引用

页码：165 / 173

页数：9

共 28 条

[21] Characterization of the binding interface between the E-domain of Staphylococcal protein A and an antibody Fv-fragment [J].