Lei Chen 阅读次数:

Lei Chen, Ph.D.

Principal Investigator

Laboratory of Structural Biology

Room 218, Wangkezhen Building,

Peking University, Beijing, China 100871

E-mail: chenlei2016@pku.edu.cn


Dr. Lei Chen received his B.S in Biology from Biological Science and Technology Department, Tsinghua University in 2005 and his Ph.D. in Biology from School of Life Science, Tsinghua University in 2010. He conducted postdoctoral research in Vollum Institute, Oregon Health and Science University from 2010 to 2016. In 2016, He joined IMM as a full-time investigator.


Selected Publications:

1. Guo W., Chen L. [Review] Recent progress in structural studies on canonical TRP ion channels. Cell Calcium (2019), 83, 102075.

2. Wu J. X., Ding D., Wang M., Chen L. [Review] Structural Insights into the Inhibitory Mechanism of Insulin Secretagogues on the Pancreatic ATP-Sensitive Potassium Channel. Biochemistry (2019).

3. Kang Y.*, Liu R.*, Wu J. X.,Chen L. Structural insights into the mechanism of human soluble guanylate cyclase. Nature (2019), 574, 206-210.

4. 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.

5. 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.

6. 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.

7. 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.

8. 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)

9. Chen, L., Dürr, KL., Gouaux, E. (2014). X-ray structures of AMPA receptor–cone snail toxin complexes illuminate activation mechanism. Science 345, 1021-1026

10. 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)

11. 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.

12. 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.

13. Liu, Y.T., Dan, Q.J., Wang, J., Feng, Y., Chen, L., Liang, J., Li, Q., Lin, S.C., Wang, Z.X., and Wu, J.W. (2011). Molecular basis of Wnt activation via the DIX domain protein Ccd1. J Biol Chem 286, 8597-8608.

14. Wang, L., Liu, Y.T., Hao, R., Chen, L., Chang, Z., Wang, H.R., Wang, Z.X., and Wu, J.W. (2011). Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP). J Biol Chem 286, 15883-15894.

15. Zhu, L., Chen, L., Zhou, X.M., Zhang, Y.Y., Zhang, Y.J., Zhao, J., Ji, S.R., Wu, J.W., and Wu, Y. (2011). Structural insights into the architecture and allostery of full-length AMP-activated protein kinase. Structure 19, 515-522.

16. 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).

17. Wang, C., Chen, L., Wang, L., Wu, J.W. (2009). Crystal structure of the MH2 domain of Drosophila Mad. Sci China C Life Sci. 52(6):539-44.

18. Hao, R., Chen, L., Wu, J.W., and Wang, Z.X. (2008). Structure of Drosophila Mad MH2 domain. Acta Crystallogr Sect F Struct Biol Cryst Commun 64, 986-990.