期刊
PROTEOMICS
卷 21, 期 21-22, 页码 -出版社
WILEY
DOI: 10.1002/pmic.202000288
关键词
carbene labelling; eIF4A; mass spectrometry; protein footprinting
资金
- Biotechnology and Biological Sciences Research Council [BB/M008770/1]
Protein-ligand interactions are crucial for cell functionality, and carbene footprinting technique can provide valuable information about these interactions, such as binding sites and conformational changes. The application of carbene footprinting to the interaction between eIF4A helicase and hippuristanol has demonstrated the potential of this technique in studying protein-ligand interactions using labeling methods.
Protein-ligand interactions are central to protein activity and cell functionality. Improved knowledge of these relationships greatly benefits our understanding of key biological processes and aids in rational drug design towards the treatment of clinically relevant diseases. Carbene footprinting is a recently developed mass spectrometry-based chemical labelling technique that provides valuable information relating to protein-ligand interactions, such as the mapping of binding sites and associated conformational change. Here, we show the application of carbene footprinting to the interaction between eIF4A helicase and a natural product inhibitor, hippuristanol, found in the coral Isis hippuris. Upon addition of hippuristanol we identified reduced carbene labelling (masking) in regions of eIF4A previously implicated in ligand binding. Additionally, we detected hippuristanol-associated increased carbene labelling (unmasking) around the flexible hinge region of eIF4A, indicating ligand-induced conformational change. This work represents further development of the carbene footprinting technique and demonstrates its potential in characterising medicinally relevant protein-ligand interactions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据