研究方向
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。我们实验室致力于研究蛋白质，特别是细胞膜整合蛋白的工作机制。目前主要研究方向为与人类健康紧密相关的一些离子通道的门控机制。我们实验室以生物学问题为导向，以结构生物学手段为主，生物化学、电生理等方法为辅来进行研究。
代表性科研论文
[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, Science345, 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.
