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膜是生命体的一种基本结构,位于其上的膜蛋白具有重要的生理功能:包括但不局限于物质转运、信号转导、催化反应等。深入理解膜蛋白工作机制对于我们理解生命过程、增进人类健康都有着重要意义。结构生物学研究室当前的主要研究方向为与代谢类疾病和心血管疾病密切相关的重要蛋白,特别是离子通道等膜蛋白的工作机制。我们主要以结构生物学、生物化学、细胞生物学、生物物理、电生理等方法来研究这些蛋白的工作机理。

研究室主任(PI)陈雷研究员 Ph.D.

Email: chenlei2016@pku.edu.cn

研究室地址:北京大学实验设备2号楼,218室

代表性文章

[1] Guo, W., Tang, Q., Wei, M., Kang, Y., Wu, J. X., and Chen, L. (2022) Structural mechanism of human TRPC3 and TRPC6 channel regulation by their intracellular calcium-binding sites, Neuron.  
[2] Niu, Y., Liu, R., Guan, C., Zhang, Y., Chen, Z., Hoerer, S., Nar, H., and Chen, L. (2021) Structural basis of inhibition of the human SGLT2-MAP17 glucose transporter, Nature 601, 280-284.
[3] Liu, R., Kang, Y., and Chen, L. (2021) Activation mechanism of human soluble guanylate cyclase by stimulators and activators, Nat Commun 12, 5492.
[4] Song, K., Wei, M., Guo, W., Quan, L., Kang, Y., Wu, J. X., and Chen, L. (2021) Structural basis for human TRPC5 channel inhibition by two distinct inhibitors, Elife 10.
[5] Wu, J. X., Liu, R., Song, K., and Chen, L. (2021) Structures of human dual oxidase 1 complex in low-calcium and high-calcium states, Nat Commun 12, 155.
[6] Guan, C., Niu, Y., Chen, S. C., Kang, Y., Wu, J. X., Nishi, K., Chang, C. C. Y., Chang, T. Y., Luo, T., and Chen, L. (2020) Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor, Nat Commun 11, 2478.
[7] Kang, Y., Wu, J. X., and Chen, L. (2020) Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex, Nat Commun 11, 6199.
[8] Wu, J. X., Ding, D., Wang, M., and Chen, L. (2020) Structural Insights into the Inhibitory Mechanism of Insulin Secretagogues on the Pancreatic ATP-Sensitive Potassium Channel, Biochemistry (Mosc.) 59, 18-25.
[9] Kang, Y., Liu, R., Wu, J. X., and Chen, L. (2019) Structural insights into the mechanism of human soluble guanylate cyclase, Nature 574, 206-210.
[10] Guo, W., and Chen, L. (2019) Recent progress in structural studies on canonical TRP ion channels, Cell Calcium 83, 102075.
[11] Ding, D., Wang, M., Wu, J. X., Kang, Y., and Chen, L. (2019) The Structural Basis for the Binding of Repaglinide to the Pancreatic KATP Channel, Cell Rep 27, 1848-1857 e1844.
[12] 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, Nat. Struct. Mol. Biol. 25, 850-858.
[13] 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.
[14] 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 Res. 28, 746-755.
[15] 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.
[16] Durr, K. L., Chen, L., Stein, R. A., De Zorzi, R., Folea, I. M., Walz, T., McHaourab, H. S., and Gouaux, E. (2014) Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states, Cell 158, 778-792.
[17] Chen, L., Durr, K. L., and Gouaux, E. (2014) X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism, Science 345, 1021-1026.
[18] Chen, L., Xin, F. J., Wang, J., Hu, J., Zhang, Y. Y., Wan, S., Cao, L. S., Lu, C., Li, P., Yan, S. F., Neumann, D., Schlattner, U., Xia, B., Wang, Z. X., and Wu, J. W. (2013) Conserved regulatory elements in AMPK, Nature 498, E8-10.
[19] 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.
[20] 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.