About James-Liu LabThe 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.
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.
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-1R17 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 20169 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
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
1. Hua T, Vemuri K, Nikas SP, Laprairie RB, Wu Y, Qu L, Pu M, Korde A, Jiang S, Ho JH, Han GW, Ding K, Li X, Liu H, Hanson MA, Zhao S, Bohn LM, Makriyannis A, Stevens RC, Liu ZJ. (2017) Crystal structures of agonist-bound human cannabinoid receptor CB1. Nature, doi: 10.1038/nature23272.
2. Song G, Yang D, Wang Y, de Graaf C, Zhou Q, Jiang S, Liu K, Cai X, Dai A, Lin G, Liu D, Wu F,5,6, Wu Y, Zhao S, Ye L, Han GW, Lau J, Wu B, Hanson MA, Liu ZJ, Wang MW, Stevens RC. (2017) Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators. Nature, doi: 10.1038/nature22378
3. Hua T, Vemuri K, Pu M, Qu L, Han GW, Wu Y, Zhao S, Shui W, Li S, Korde A, Laprairie RB, Stahl EL, Ho JH, Zvonok N, Zhou H, Kufareva I, Wu B, Zhao Q, Hanson MA, Bohn LM, Makriyannis A, Stevens RC, Liu ZJ. (2016) Crystal Structure of the Human Cannabinoid Receptor CB1. Cell, doi: 10.1016/j.cell.2016.10.004
4. Li J, Rodriguez JP, Niu F, Pu M, Wang J, Hung LW, Shao Q, Zhu Y, Ding W, Liu Y, Da Y, Yao Z, Yang J, Zhao Y, Wei GH, Cheng G, Liu ZJ, Ouyang S. (2016) Structural basis for DNA recognition by STAT6. PNAS, doi: 10.1073/pnas.1611228113.
5. Batyuk A, Galli L, Ishchenko A, Han GW, Gati C, Popov PA, Lee MY, Stauch B, White TA, Barty A, Aquila A, Hunter MS, Liang M, Boutet S, Pu M, Liu ZJ, Nelson G, James D, Li C, Zhao Y, Spence JC, Liu W, Fromme P, Katritch V, Weierstall U, Stevens RC, Cherezov V. (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 X, Liu J, Shi Q, Tan Q, Wu D, Skinner JJ, Walker AL, Zhao L, Gu X, Chen N, Xue L, Si P, Zhang L, Wang Z, Katritch V, Liu ZJ, Stevens RC. (2016) In vitro expression and analysis of the 826 human G protein-coupled receptors. Protein Cell, doi: 10.1007/s13238-016-0263-8
7. Gu J, Feng Y, Feng X, Sun C, Lei L, Ding W, Niu F, Jiao L, Yang M, Li Y, Liu X, Song J, Cui Z, Han D, Du C, Yang Y, Ouyang S, Liu ZJ, Han W. (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 L, Mo J, Swanson KV, Wen H, Petrucelli A, Gregory SM, Zhang Z, Schneider M, Jiang Y, Fitzgerald KA, Ouyang S, Liu ZJ, Damania B, Shu HB, Duncan JA, Ting JP. (2014) NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immunesignaling induced by the DNA sensor STING. Immunity, doi: 10.1016/j.immuni.2014.01.010
9. Natashin PV, Ding W, Eremeeva EV, Markova SV, Lee J, Vysotski ES, Liu ZJ.. (2014) Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and afterbioluminescence support the catalytic function of a water molecule in the reaction. Acta Crystallogr D Biol Crystallogr, doi: 10.1107/S1399004713032434
10. Won EY, Xie Y, Takemoto C, Chen L, Liu ZJ, Wang BC, Lee D, Woo EJ, Park SG, Shirouzu M, Yokoyama S, Kim SJ, Chi SW. (2013) High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26. Acta Crystallogr D Biol Crystallogr, doi: 10.1107/S0907444913004770
11. Jiao L, Ouyang S, Liang M, Niu F, Shaw N, Wu W, Ding W, Jin C, Peng Y, Zhu Y, Zhang F, Wang T, Li C, Zuo X, Luan CH, Li D, Liu 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 H, Ni X, Zhao L, Crowley C, Ding W, Hung LW, Shaw N, Cheng G, Liu ZJ. (2013) Structural basis for termination of AIM2-mediated signaling by p202. Cell Research, doi: 10.1038/cr.2013.52
13. Niu F, Shaw N, Wang YE, Jiao L, Ding W, Li X, Zhu P, Upur H, Ouyang S, Cheng G, Liu ZJ. (2013) Structure of the Leanyer Orthobunyavirus Nucleoprotein-RNA complex reveals novel architecture for RNA encapsidation. PNAS, doi: 10.1073/pnas.1300035110
14. Parvatiyar K, Zhang Z, Teles RM, Ouyang S, Jiang Y, Iyer SS, Zaver SA, Schenk M, Zeng S, Zhong W, Liu ZJ, Modlin RL, Liu YJ, Cheng 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.Nat Immunol, doi: 10.1038/ni.2460
15. Zhan Z, Ouyang S, Liang W, Zhang Z, Liu ZJ, Huang L. (2012) Structural and functional characterization of the C-terminal catalytic domain of the SSV1 integrase. Acta Cryst, doi: 10.1107/S0907444912007202
16. Ru H, Zhao L, Ding W, Jiao L, Shaw N, Liang W, Zhang L, Hung LW, Matsugaki N, Wakatsuki S, Liu ZJ. (2012) The S-SAD phasing study of DR6 and its solution conformation revealed by SAXS. Acta Cryst, doi: 10.1107/S0907444912004490
17. Liu ZJ, Chen L, Wu D, Ding W, Zhang H, Zhou W, Fu ZQ, Wang BC. (2011) A multi-dataset data-collection strategy produces better diffraction data. Acta Crystallogr A, doi: 10.1107/S0108767311037469
18. Wu D, Li Y, Song G, Cheng C, Zhang R, Joachimiak A, Shaw N, Liu 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 N, Zhao M, Cheng C, Xu H, Saarikettu J, Li Y, Da Y, Yao Z, Silvennoinen O, Yang J, Liu ZJ, Wang BC, Rao Z. (2007) The multifunctional human p100 protein 'hooks' methylated ligands. Nat Struct Mol Biol, doi: 10.1038/nsmb1269
20. Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S. (2007). Curved EFC/F-BAR domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell, doi: 10.1016/j.cell.2007.03.040
21. Liu ZJ, Stepanyuk GA, Vysotski ES, Lee J, Markova SV, Malikova NP, Wang 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 ZJ, Tempel W, Ng JD, Lin D, Shah AK, Chen L, Horanyi PS, Habel JE, Kataeva IA, Xu H, Yang H, Chang JC, Huang L, Chang SH, Zhou W, Lee D, Praissman JL, Zhang H, Newton MG, Rose JP, Richardson JS, Richardson DC, Wang BC. (2005). The high-throughput protein-to-structure pipeline at SECSG. Acta Cryst D, doi: 10.1107/S0907444905013132
23. Liu ZJ, Lin D, Tempel W, Praissman JL, Rose JP, Wang BC. (2005) Parameter-space screening: a powerful tool for high-throughput crystal structure determination. Acta Cryst D, doi: 10.1107/S0907444905003239
24. Liu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC. (1997). The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. Nat Struct Biol, 1997 Apr;4(4):317-26.
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