Clore G M, Gronenborn A M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
Protein Sci. 1994 Mar;3(3):372-90. doi: 10.1002/pro.5560030302.
The recent development of a whole panoply of multidimensional heteronuclear-edited and -filtered NMR experiments has revolutionized the field of protein structure determination by NMR, making it possible to extend the methodology from the 10-kDa limit of conventional 2-dimensional NMR to systems up to potentially 35-40 kDa. The basic strategy for solving 3-dimensional structures of larger proteins and protein-ligand complexes in solution using 3- and 4-dimensional NMR spectroscopy is summarized, and the power of these methods is illustrated using 3 examples: interleukin-1 beta, the complex of calmodulin with a target peptide, and the specific complex of the transcription factor GATA-1 with its cognate DNA target site.
最近一系列多维异核编辑和过滤核磁共振实验的发展彻底改变了通过核磁共振确定蛋白质结构的领域,使得该方法能够从传统二维核磁共振的10 kDa极限扩展到潜在可达35 - 40 kDa的系统。总结了使用三维和四维核磁共振光谱法在溶液中解析较大蛋白质和蛋白质 - 配体复合物三维结构的基本策略,并通过三个例子说明了这些方法的强大之处:白细胞介素 - 1β、钙调蛋白与靶肽的复合物以及转录因子GATA - 1与其同源DNA靶位点的特异性复合物。