GENG Yong
Principal Investigator
Research Center for Structure and Function of Drug Targets
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CONTACT
gengyong@simm.ac.cn
021-50800570
201203
Shanghai Institute of Materia Medica, Chinese Academy of Sciences
Biography
Education
2003-2006 Institute of Biophysics, Chinese Academy of Sciences, Beijing, China Ph.D. in Molecular Biology
2000-2003 China Pharmaceutical University, Nanjing, China M.S. in Medicinal Chemistry
1993-1997 HuBei Medical University, Hubei, China B.S. in Pharmacology
Research Experience
2016-present Professor, Shanghai Institute of Materia Medica, CAS
2009-2015 Postdoctoral Research Scientist, Columbia University
2007-2009 Postdoctoral Research Scientist, Dartmouth Medical School
2003-2006 Graduate Student, Institute of Biophysics, Chinese Academy of Sciences
2000-2003 Master Student, China Pharmaceutical University
Research Directions
Our current research is focused on the structure and function of cell surface receptors and drug discovery. We combine x-ray crystallography and Cryo-EM with biochemical techniques to determine the specificity of receptor-ligand interactions, and to identify receptor activation mechanisms. We also design the receptor based on their structure as antigen to improve the efficiency of antibody and nanobody discovery for therapeutic applications.
Grants & Research Projects
Achievements
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Social Titles
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Awards & Honors
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Pubilcations
Full Publication List
Selected Publications
1. Geng, Y., Bush, M., Mosyak, L., Wang, F., and Fan, Q.R. (2013). Structural mechanism of ligand activation in human GABAB receptor. Nature 504, 254-259.
2.Hao Zuoa, Ian Glaasera, Yong Geng#, Paul A. Slesinger#and Qing R. Fan#（2019）Structural basis for auxiliary subunit KCTD16 regulation of the GABAB receptor. Proc. Nat. Acad. Sci. USA 116，8370–8379 (# co-responding author)
3.Geng, Y., Mosyak L, Kurinov I, Zuo H, Sturchler E, Cheng TC, Subramanyam P, Brown AP, and Fan, Q.R. (2016).Structural mechanism of ligand activation in human calcium-sensing receptor. eLife 5, e13662.
4. Burmakina, S.*, Geng, Y.*, Chen, Y., and Fan, Q.R. (2014). Heterodimeric coiled-coil interactions of human GABAB receptor. Proc. Nat. Acad. Sci. USA 111, 6958-63. (*Equal contribution).
5. Geng, Y., Xiong, D., Mosyak, L., Malito, D. L., Kniazeff, J., Chen, Y., Burmakina, S., Quick, M., Bush, M., Javitch, J. A., Pin, J.-P., and Fan, Q. R. (2012). Structure and functional interaction of the extracellular domain of human GABAB receptor GBR2. Nature Neuroscience,15, 970-978.
6. Feng, Y.*, Geng, Y.*, Zhou, T., Wang, J. (2012). NMR structure note: human esophageal cancer-related gene 2. J Biomol NMR 53, 65-70. (*Equal contribution).
7. Chang, C.C., Miyazaki, A., Dong, R., Kheirollah, A., Yu, C., Geng, Y., Higgs, H.N. and Chang T.Y. (2010). Purification of recombinant acyl-coenzyme A:cholesterol acyltransferase 1 (ACAT1) from H293 cells and binding studies between the enzyme and substrates using difference intrinsic fluorescence spectroscopy. Biochemistry 49:9957-63.
8. Geng, Y*., Feng, Y*., Xie, T., Shan, L. and Wang, J. (2009). The native-like interactions between SNase121 and SNase(111-143) fragments induce the recovering their native-like structures and the ability to degrade DNA. Biochemistry 48, 8692–8703. (*Equal contribution).
9. Urano, Y., Watanabe, H., Murphy, S.R., Shibuya, Y., Geng, Y., Peden, A.A., Chang, C.C. and Chang, T.Y. (2008). Transport of LDL-derived cholesterol from the NPC1 compartment to the ER involves the trans-Golgi network and the SNARE protein complex. Proc. Nat. Acad. Sci. USA 105, 16513-8.
10. Geng, Y., Feng, Y., Xie, T., Dai, Y., Wang J. and Lu, S. (2008). Mapping the putative binding site for uPA protein in Esophageal Cancer-Related Gene 2 by heteronuclear NMR method. Arch. Biochem. and Biophys. 479, 153-157.
11. Geng, Y., Wang, M., Xie, T. and Wang, J. (2007). Folding of the C-terminal fragment V111-D143 of staphylococcal nuclease in aqueous solution. Protein Pept. Lett. 14, 747-55.
12. Geng,Y., Zhou J., Isolation and Identification of Steroid Saponins from the Fresh Rhizomes of Dioscorea Panthaica. (2004). Chinese J. Nat. Med. 2, 25-27.
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