On December 12, the Biological Microstructure Research Platform of our institute, in collaboration with the team of Daohua Jiang from the Institute of Physics of the Chinese Academy of Sciences, and Yan Zhao’s team from the Institute of Biophysics of the Chinese Academy of Sciences, used cryo-electron microscopy single-particle reconstruction technology to acquire high-resolution structures of Vesicular Monoamine Transporter 2 (VMAT2) in different conformations. This revealed the conformational changes and transport mechanisms of VMAT2 in the process of transporting monoamine substrates. The research, titled "Transport and inhibition mechanisms of human VMAT2", was published in Nature.

The research provides an essential structural foundation for understanding the molecular mechanisms of substrate recognition, drug inhibition, and proton-coupled transport processes of VMAT2. This knowledge will offer vital structural information for the development of conformation-specific and subtype-specific drugs targeting VMAT2. Furthermore, the methods employed to analyze VMAT2 (a mere 56 kilodaltons) in this study can be applied to other small membrane proteins, contributing to electron microscopy structural analyses of membrane transport proteins and other small proteins.