Dr. Nieng Yan

Dr. Nieng Yan

Principal Investigator
Shenzhen Medical Academy of Research and Translation
(SMART)
School of Life Sciences
Tsinghua University
BioGRAPHY

Dr. Nieng Yan received her B.S. degree from the Department of Biological Sciences & Biotechnology, Tsinghua University, Beijing, China, in 2000. She then pursued her PhD in the Department of Molecular Biology at Princeton University under the supervision of Prof. Yigong Shi between 2000 and 2004. She was the regional winner of the Young Scientist Award (North America) co-sponsored by Science/AAAS and GE Healthcare in 2005 for her thesis on the structural and mechanistic study of programmed cell death. She continued her postdoctoral training at Princeton University, focusing on the structural characterization of intramembrane proteases. In 2007, she joined the faculty of School of Medicine, Tsinghua University. Her lab has been mainly focusing on the structural and functional study of membrane transport proteins exemplified by the glucose transporters and Na+/Ca2+ channels. In 2012 and 2013, she was promoted to tenured professor and Bayer Endowed Chair Professor, respectively. Dr. Yan was an HHMI international early career scientist in 2012-2017, the recipient of the 2015 Protein Society Young Investigator Award and the 2015 Beverley & Raymond Sackler International Prize in Biophysics, and the Alexander M. Cruickshank lecturer at the GRC on membrane transport proteins in 2016.

Speaker's Schedule

Dec 22, 2022
09:20 - 10:00
Society Lecture | Live from Hangzhou site
Targeting Nav channels for pain relief
Voltage-gated sodium (Nav) channels are responsible for the initiation and propagation of action potentials. Associated with a variety of disorders, Nav channels are targeted by multiple pharmaceutical drugs and natural toxins. Employing the modern methods of cryo-EM, we determined high resolution structures of a number of eukaryotic and eventually human Nav channels in complex with auxiliary subunits, toxins, and drugs, which reveal the mode of action of representative Nav modulators. Based on the structural discovery, we suggest a "door-wedge" allosteric blocking mechanism for fast inactivation of Nav channels. Structural comparison of the conformationally distinct Nav channels provides important insights into the electromechanical coupling mechanism of Nav channels, offers the 3D template to map hundredes of disease mutations, and will aid rational design of next-generation pain killers.
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