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Email: chenlei2016(at)pku(dot)edu(dot)cn 

Research interestStructural Biology

Office: Rm.218, Wang Kezhen Building, Peking University


Research Area:

My research aims to understand how proteins work, especially integral membrane proteins. These protein play important roles in many biological processes, such as material transport, signal transduction and catalytic reaction. Understanding how those molecules work in atomic details is essential for us to manipulate their activity and improve human health. One major focus of our lab is on the gating mechanism of ion channels which are important drug targets and implicated in human diseases. For example, the energy sensors ATP-sensitive potassium channels (KATP) can couple intracellular energy status to cell excitability and gate insulin release in pancreatic beta cells. We are currently using structural biology tools combined with biochemistry and electrophysiology methods to elucidate how those channels work.


Selected Publications:

1.    Zhang, M., Wang, D., Kang, Y., Wu, J.X., Yao, F., Pan, C., Yan, Z.#, Song, C.#, and Chen, L.# (2018). Structure of the mechanosensitive OSCA channels. Nature structural & molecular biology 25, 850-858.
2.    Tang, Q.*, Guo, W.*, Zheng, L., Wu, J.X., Liu, M., Zhou, X., Zhang, X.#, and Chen, L.# (2018). Structure of the receptor-activated human TRPC6 and TRPC3 ion channels. Cell research.
3.    Wu, J.X., Ding, D., Wang, M., Kang, Y., Zeng, X., and Chen, L. (2018). Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels. Protein Cell 9, 553-567.
4.    Li, N.*, Wu, J.X.*, Ding, D., Cheng, J., Gao, N.#, and Chen, L#. (2017). Structure of a Pancreatic ATP-Sensitive Potassium Channel. Cell 168, 101-110 e110.(# Co-corresponding author)
5.    Chen, L., Dürr, KL., Gouaux, E. (2014). X-ray structures of AMPA receptor–cone snail toxin complexes illuminate activation mechanism. Science 345, 1021-1026
6.    Dürr, KL.*, Chen, L.*, Stein, RA., De Zorzi, R., Folea, IM., Walz, T., Mchaourab, HS., Gouaux, E. (2014). Structure and Dynamics of AMPA Receptor GluA2 in Resting, Pre-Open, and Desensitized States. Cell 158,  778–792  (*Co-first author)
7.    Chen, L., Xin, F.J., Wang, J., Hu, J., Zhang, Y.Y., Wan, S., Cao, L.S., Lu, C., Li, P., Yan, S.F., et al. (2013). Conserved regulatory elements in AMPK. Nature 498, E8-10.
8.    Chen, L., Wang, J., Zhang, Y.Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.X., and Wu, J.W. (2012). AMP-activated protein kinase undergoes nucleotide-dependent conformational changes. Nat Struct Mol Biol 19, 716-718.
9.    Chen, L.,* Jiao, Z.H.*, Zheng, L.S.*, Zhang, Y.Y., Xie, S.T., Wang, Z.X., and Wu, J.W. (2009). Structural insight into the autoinhibition mechanism of AMP-activated protein kinase. Nature 459, 1146-1149. (*Co-first author)

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