About James-Liu Lab

The iHuman Institute is a new international effort established as a research institute located on the campus of ShanghaiTech University. The institute is a gateway to the world of Shanghai life science research. What makes the iHuman Institute special is that it is focused exclusively on the basic and applied science of human cell signaling, integrating multiple tools for scientific discovery, and bringing together leading researchers throughout the world. Cell surface receptors and their related intracellular proteins are responsible for human cellular communications with each other and their environment, and are involved in a wide range of physiological activities. Such a central role in human biology makes cell signaling the target for intervention for tuning physiological responses and fighting numerous conditions and diseases. These proteins are central to understanding the evolution of mankind and human cognition at a molecular level.

People

Zhi-Jie Liu Professor, Deputy Director


iHuman Institute is a new international effort established as a research institute located on the campus of ShanghaiTech University. The institute is a gateway to the world of Shanghai life science research. What makes iHuman Institute special is that it is focused exclusively on the basic and applied science of human cell signaling, integrating multiple tools for scientific discovery, and bringing together leading researchers throughout the world.

Gaojie Song
Natashin Pavel
Yuxia Wang
Hua Tian
Peng Yao
Qu Lu
Yang Yang
Xiaoting Li
Zhijie Xu
Jingjing Wang
Kaiwen Liu
Wu Meng
Shen Ling
Mengyang Xu

News

Student with a Dream Publishes Agonist-bound Marijuana Receptor Structure in Nature

6 Jul, 2017

July 6, 2017 — A team of scientists led by Professor Zhi-jie Liu at the iHuman Institute of ShanghaiTech University has determined the 3-dimensional molecular structure of the agonist-bound human cannabinoid receptor CB1. The work reveals the structural features of agonist-bound CB1 and the activation mechanism of the receptor. The results, described in a paper entitled “Crystal structures of agonist-bound human cannabinoid receptor CB1”, published online on July 6, 2017 in the prestigious journal Nature....Read more

Key Diabetes Receptor Structure Determined by International Collaboration—Shanghai Led Consortium Produces High Resolution 3D map of GLP-1R

17 May, 2017

May 17, 2017 — An international team led by the iHuman Institute, ShanghaiTech University has determined the 3-dimensional molecular structure of the human glucagon-like peptide-1 receptor (GLP-1R) drug binding domain. The work reveals molecular mechanisms of allosteric regulation in class B G protein-coupled receptors (GPCRs). The results, described in a paper entitled “Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators”, is published online on May 17, 2017 in the journal Nature. This paper is published simultaneously with a companion paper led by colleagues at the Shanghai Institute of Materia Medica (SIMM) describing the full-length glucagon receptor in the same journal....Read more

iHuman Institute Scientific Research Selected as Shanghai Top Ten Science & Technology Stories for 2016

9 Jan, 2017

January 9, 2017 – The Shanghai city government recently announced the 2016 Shanghai Top Ten Science & Technology stories. Included in the list is the structure of cannabinoid receptor 1 (CB1), also known as the “marijuana receptor” published in the prestigious international journal Cell in October, 2016....Read more

ShanghaiTech Scientists Resolve the Structure of the Human “Marijuana Receptor”

20 Oct, 2016

October 20, 2016 – A team of scientists led by the iHuman Institute of ShanghaiTech University has determined and analyzed the high-resolution atomic structure of human cannabinoid receptor 1 (CB1), also known as the “marijuana receptor”. This new findings provide clues to understand why some drugs that interact with this receptor have had unexpectedly complex and sometimes harmful effects, while the utility of the crystal structure may provide inspiration for drug design toward refining efficacy and avoiding adverse effects....Read more


Selected Publications

1. Hua T1,2,3Vemuri K4Nikas SP4Laprairie RB5Wu Y1Qu L1,2,3Pu M1Korde A4Jiang S4Ho JH5Han GW6Ding K1,3,7Li X8Liu H8Hanson MA9Zhao S1,7Bohn LM5Makriyannis A4Stevens RC1,6,7Liu ZJ1,2,7. (2017) Crystal structures of agonist-bound human cannabinoid receptor CB1. , doi: 10.1038/nature23272.

2. Song G1Yang D2Wang Y1de Graaf C3Zhou Q1Jiang S4Liu K1,5,6Cai X2Dai A2Lin G5Liu D1Wu F1,5,6Wu Y1Zhao S1,5Ye L4Han GW7Lau J8Wu B5,6,9Hanson MA10Liu ZJ1,5,11Wang MW2,4,5Stevens RC1,5. (2017) Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators. , doi: 10.1038/nature22378

3. Hua T1Vemuri K2Pu M3Qu L1Han GW4Wu Y5Zhao S5Shui W5Li S5Korde A2Laprairie RB6Stahl EL6Ho JH6Zvonok N2Zhou H2Kufareva I7Wu B8Zhao Q8Hanson MA9Bohn LM10Makriyannis A11Stevens RC12Liu ZJ13. (2016) Crystal Structure of the Human Cannabinoid Receptor CB1. , doi: 10.1016/j.cell.2016.10.004

4. Li J1,2Rodriguez JP3Niu F1Pu M1Wang J4Hung LW5Shao Q4Zhu Y1Ding W1Liu Y1Da Y6Yao Z6Yang J6Zhao Y1Wei GH7Cheng G3Liu ZJ1,6,8,9Ouyang S10,3. (2016) Structural basis for DNA recognition by STAT6. PNAS, doi: 10.1073/pnas.1611228113.

5. Batyuk A1Galli L2Ishchenko A3Han GW3Gati C2Popov PA4Lee MY3Stauch B3White TA2Barty A2Aquila A5Hunter MS5Liang M5Boutet S5Pu M6Liu ZJ7Nelson G8James D8Li C8Zhao Y8Spence JC8Liu W9Fromme P9Katritch V10Weierstall U8Stevens RC11Cherezov V12. (2016) Native Phasing of X-ray Free Electron Laser data for a G protein-coupled receptor. Science Advances, doi: 10.1126/sciadv.1600292

6. Lv X1Liu J1Shi Q1Tan Q1Wu D1Skinner JJ1Walker AL2Zhao L1Gu X1Chen N1Xue L1Si P1Zhang L1Wang Z1Katritch V2Liu ZJ1Stevens RC3. (2016) In vitro expression and analysis of the 826 human G protein-coupled receptors. , doi: 10.1007/s13238-016-0263-8

7. Gu J1Feng Y2Feng X1Sun C1Lei L1Ding W3Niu F4Jiao L4Yang M1Li Y1Liu X1Song J1Cui Z1Han D1Du C1Yang Y1Ouyang S4Liu ZJ4Han W1. (2014) Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin. PLOS Pathogens, doi: 10.1371/journal.ppat.1004109

8. Zhang L1Mo J2Swanson KV3Wen H3Petrucelli A3Gregory SM3Zhang Z3Schneider M4Jiang Y5Fitzgerald KA6Ouyang S5Liu ZJ7Damania B8Shu HB9Duncan JA2Ting JP10. (2014) NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immunesignaling induced by the DNA sensor STING. , doi: 10.1016/j.immuni.2014.01.010

9. Natashin PV1Ding W1Eremeeva EV2Markova SV2Lee J3Vysotski ES2Liu ZJ1.. (2014) Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and afterbioluminescence support the catalytic function of a water molecule in the reaction. , doi: 10.1107/S1399004713032434

10. Won EY1Xie YTakemoto CChen LLiu ZJWang BCLee DWoo EJPark SGShirouzu MYokoyama SKim SJChi SW. (2013) High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26. , doi: 10.1107/S0907444913004770

11. Jiao L1Ouyang SLiang MNiu FShaw NWu WDing WJin CPeng YZhu YZhang FWang TLi CZuo XLuan CHLi DLiu ZJ. (2013) Structure of severe fever with thrombocytopenia syndrome virus nucleocapsid protein in complex with suramin reveals therapeutic potential. J. Virology, doi: 10.1128/JVI.00672-13

12. Ru HNi XZhao LCrowley CDing WHung LWShaw NCheng GLiu ZJ. (2013) Structural basis for termination of AIM2-mediated signaling by p202. Cell Research, doi: 10.1038/cr.2013.52

13. Niu F1Shaw NWang YEJiao LDing WLi XZhu PUpur HOuyang SCheng GLiu ZJ. (2013) Structure of the Leanyer Orthobunyavirus Nucleoprotein-RNA complex reveals novel architecture for RNA encapsidation. PNAS, doi: 10.1073/pnas.1300035110

14. Parvatiyar K1Zhang ZTeles RMOuyang SJiang YIyer SSZaver SASchenk MZeng SZhong WLiu ZJModlin RLLiu YJCheng G. (2012) The helicase DDX41 recognizes the bacterial secondary messengers cyclic di-GMP and cyclic di-AMP to activate a type I interferon immune response., doi: 10.1038/ni.2460

15. Zhan Z1Ouyang SLiang WZhang ZLiu ZJHuang L. (2012) Structural and functional characterization of the C-terminal catalytic domain of the SSV1 integrase. Acta Cryst, doi: 10.1107/S0907444912007202 

16. Ru H1Zhao LDing WJiao LShaw NLiang WZhang LHung LWMatsugaki NWakatsuki SLiu ZJ. (2012) The S-SAD phasing study of DR6 and its solution conformation revealed by SAXS. Acta Cryst, doi: 10.1107/S0907444912004490

17. Liu ZJ1Chen LWu DDing WZhang HZhou WFu ZQWang BC. (2011) A multi-dataset data-collection strategy produces better diffraction data. , doi: 10.1107/S0108767311037469

18. Wu D1Li YSong GCheng CZhang RJoachimiak AShaw NLiu ZJ. (2009) Structural basis for the inhibition of human MTHFS by N10-substituted folate analogues. Cancer Research, doi: 10.1158/0008-5472.CAN-09-1927

19. Shaw N1Zhao MCheng CXu HSaarikettu JLi YDa YYao ZSilvennoinen OYang JLiu ZJWang BCRao Z. (2007) The multifunctional human p100 protein 'hooks' methylated ligands. , doi: 10.1038/nsmb1269

20. Shimada A1Niwa HTsujita KSuetsugu SNitta KHanawa-Suetsugu KAkasaka RNishino YToyama MChen LLiu ZJWang BCYamamoto MTerada TMiyazawa ATanaka ASugano SShirouzu MNagayama KTakenawa TYokoyama S. (2007). Curved EFC/F-BAR domain dimers are joined end to end into a filament for membrane invagination in endocytosis. , doi: 10.1016/j.cell.2007.03.040

21. Liu ZJ1Stepanyuk GAVysotski ESLee JMarkova SVMalikova NPWang BC. (2006). Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state. PNAS, doi: 10.1073/pnas.0511142103

22. Liu ZJ1Tempel WNg JDLin DShah AKChen LHoranyi PSHabel JEKataeva IAXu HYang HChang JCHuang LChang SHZhou WLee DPraissman JLZhang HNewton MGRose JPRichardson JSRichardson DCWang BC. (2005). The high-throughput protein-to-structure pipeline at SECSG. Acta Cryst D, doi: 10.1107/S0907444905013132

23. Liu ZJ1Lin DTempel WPraissman JLRose JPWang BC. (2005) Parameter-space screening: a powerful tool for high-throughput crystal structure determination. Acta Cryst D, doi: 10.1107/S0907444905003239

24. Liu ZJ1Sun YJRose JChung YJHsiao CDChang WRKuo IPerozich JLindahl RHempel JWang BC. (1997). The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. , 1997 Apr;4(4):317-26.

Contact us

Address: Building No.6 99 HaiKe Rd, Zhangjiang High Tech Park Pudong District, Shanghai 201210


Tel: (86)21 20685005


Email: ihuman@shanghaitech.edu.cn