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Lecture Title | Structural basis for ATP binding and activation of P2X receptors |
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Date | 2012/04/11 (Wed) 15:00 ~ 17:00 |
Lecturer | Dr. Motoyuki Hattori, Postdoc, Oregon Health&Science University, Vollum Institute, Eric Gouaux lab. |
Place | Yamate Building 3, 2nd floor, Seminar Room |
Summary | Adenosine-5'-triphosphate (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 ATP-activated ion channels permeable to Na+, K+ and Ca2+, expressed throughout the human body including the nervous, cardiovascular and immune systems and are implicated in various physiological processes such as synaptic transmission, smooth muscle contraction, taste, nociception and inflammation. A recent crystal structure of the P2X4 receptor in an apo, closed state, revealed the chalice-shaped trimeric architecture of P2X receptors. 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. In this seminar, I will present our new structures of the P2X receptor and discuss the mechanism of agonist binding and activation of P2X receptors. |
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Oregon Health&Science University, Vollum Institute, Eric Gouaux lab. |