报告题目：Mechanism of ligand recognition and activation of ATP-gated P2X cation channels

报 告 人： Dr. Motoyuki Hattori

The University of Tokyo

Graduate School of Science

Department of Biophysics and Biochemstry

报告时间：4月18日下午13:30

报告地点：闵行校区生物药学楼2-116会议室

Abstract: ATP is known as the vital energy source involved in energy metabolism, biosynthetic reactions and active transport. It is also an essential extracellular signaling molecule that activates two distinct families of ATP receptors: ionotropic P2X and G-protein-coupled P2Y receptors. P2X receptors are trimeric non-selective cation channels involved in various physiological processes including synaptic transmission, taste, neuronal pain and inflammation. A recent crystal structure of zebrafish P2X4 receptor in an apo, closed state, revealed the chalice-shaped trimeric architecture of P2X receptors (Kawate et.al. Nature 2009). However, due to the lack of a crystal structure in complex with ATP, the agonist binding site and the mechanism of channel activation remained unclear. I will present the agonist-bound structures of zebrafish P2X4 receptor and discuss the mechanism of ligand binding and activation of P2X receptors (Hattori & Gouaux Nature 2012).