Ferrage Fabien, Dutta Kaushik, Cowburn David
New York Structural Biology Center, New York, NY 10027, USA.
Department of Chemistry, École Normale Supérieure-PSL Research University, 24 rue Lhomond, 75005 Paris, France.
Molecules. 2015 Dec 9;20(12):21992-9. doi: 10.3390/molecules201219824.
The proper characterization of protein-ligand interfaces is essential for structural biology, with implications ranging from the fundamental understanding of biological processes to pharmacology. Nuclear magnetic resonance is a powerful technique for such studies. We propose a novel approach to the direct determination of the likely pose of a peptide ligand onto a protein partner, by using frequency-selective cross-saturation with a low stringency isotopic labeling methods. Our method illustrates a complex of the Src homology 3 domain of C-terminal Src kinase with a peptide from the proline-enriched tyrosine phosphatase.
蛋白质-配体界面的正确表征对于结构生物学至关重要，其影响范围从对生物过程的基本理解到药理学。核磁共振是用于此类研究的强大技术。我们提出了一种新方法，通过使用具有低严格度同位素标记方法的频率选择性交叉饱和，直接确定肽配体在蛋白质伴侣上的可能构象。我们的方法展示了C端Src激酶的Src同源3结构域与富含脯氨酸的酪氨酸磷酸酶的一种肽形成的复合物。
