研究团队
丁建平
研究员,研究组长,博士生导师
邮箱:  jpding@@sibcb.ac.cn
电话:  021-20776082
他/她的实验室

个人简介:
        1982年1月南京大学获理学学士学位;1984年10月中山大学获理学硕士学位;1987年10月复旦大学获理学博士学位。1987年11月至1989年6月,中国科学院上海硅酸盐研究所博士后。1989年7月至1991年8月,联邦德国柏林自由大学结晶学研究所洪堡基金会奖研金学者。1991年9月至2000年10月,美国新泽西州罗格斯大学,先后任化学与化学生物学系研究助理、研究助理教授、研究副教授。2000年11月起,任中科院上海生科院生化与细胞所研究员、博士生导师。获得中科院“百人计划”(2000年)和国家杰出青年基金(2001年)资助,2006年入选国家人事部“新世纪百千万人才工程”国家级人选。主要学术任职包括:“国际蛋白质数据库”顾问委员会(Worldwide-PDB Advisory Committee)委员(2010年-今);“亚洲晶体学会”理事(2006年-今);“中国晶体学会”常务理事(2003年-今)、“生物大分子专业委员会” 副主任委员(2012年-今);“中国生物物理学会”副理事长和常务理事(2009年-今);“上海市生物物理学会”常务理事(2006年-今)、理事长(2014年-今)、“分子生物物理和结构生物学专业委员会” 主任委员(2006年-今)、 “中国生物化学与分子生物学会”“蛋白质组学专业委员会”副主任委员(2007年-今);“上海市生物化学与分子生物学会”常务理事(2008年-今)、副理事长(2011年-今)等。英国《BMC Structural Biology》副主编(2008年-2011年)、晶体学部主编(2011年-今);《Biochemical Journal》编辑顾问委员会委员(2004年-今);中国《生物化学与生物物理学报》编委(2006年-今);《生物化学与生物物理进展》编委(2005年-今);《生命的化学》编委(2006年-今)等。


研究方向:

        真核基因表达调控的结构生物学

研究工作:

        真核生物的基因表达是一个非常复杂的过程,在基因转录、mRNA加工和运输、蛋白质翻译等多个层次上受到多种方式的调控,表达调控的异常会导致细胞的非正常发育和分化,产生多种疾病包括肿瘤。我们研究组主要围绕一系列参与染色质修饰、mTOR信号转导通路、DNA损伤修复通路和生物代谢过程的重要蛋白质和蛋白质复合物,运用结构生物学、分子生物学、生物化学、细胞生物学等方法,开展蛋白质的结构、功能及其分子机制的研究。我们希望这些研究工作不仅能促进人们对参与真核基因表达调控的一些重要蛋白质的生物功能、分子机理、结构和功能关系的认识,同时也能为探索与这些蛋白质的功能失调相关疾病的发病机理、寻找疾病诊断的新靶标和新方法、设计和研发治疗疾病的药物等奠定分子基础。近年来主持、参与并完成国家、科学院和地方政府的多项重大研究项目。在国际重要学术刊物上发表研究论文150多篇,近五年来发表研究论文40多篇,其中包括Science、Nature、Nature Struct Mol Biol、Blood、PNAS、EMBO J、Cell Res、eLife、Nucleic Acids Res、J Biol Chem、Structure、Biochem J等。


2010年至今发表的代表性研究论文(*通讯作者):

(1) Wenjing Li, Tianlong Zhang, and Jianping Ding* “Molecular basis for the substrate specificity and catalytic mechanism of thymine-7-hydroxylase in fungi”, Nucleic Acids Res., doi: 10.1093/nar/gkv979, Epub Oct 1 (2015).
(2) Shaoqiong Xu$, Tianlong Zhang$, Shiva N. Kompella$, Mengdi Yan, Aiping Lu, Yanfang Wang, Xiaoxia Shao, Chengwu Chi, David J. Adams*, Jianping Ding*, and Chunguang Wang* “Conotoxin aD-GeXXA utilizes a novel strategy to antagonize nicotinic acetylcholine receptors”, Sci. Rep., 5: 14261 (2015). ($Contributed equally)
(3) Qingyu Tang, Caifeng Liu, Chen Zhong, and Jianping Ding* “Crystal structures of Arabidopsis thaliana Nudix hydrolase NUDT7 reveal a previously unobserved conformation”, Mol. Plant, 8: 1557-1559 (2015).
(4) Katie Powis$, Tianlong Zhang$, Nicolas Panchaud, Rong Wang, Claudio De Virgilio*, and Jianping Ding* “Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling”, Cell Res., 25: 1043-59 (2015). ($Contributed equally)
(5) Fang Yu$, Fangyuan He$, Hongyan Yao, Chengyuan Wang, Jianchuan Wang, Jianxu Li, Xiaofeng Qi, Hong-Wei Xue*, Jianping Ding*, and Peng Zhang* “Structural basis of intramitochondrial phosphatidic acid transport mediated by the Ups1-Mdm35 complex”, EMBO Rep., 16: 813-823 (2015). ($Contributed equally)
(6) Lun Zhang, Jianchuan Wang, Li Hou, Pengrong Cao, Li Wu, Qiansen Zhang, Huaiyu Yang, Yi Zhang*, Jianping Ding* and Jia Li* “Functional role of histidine in the conserved His-x-Asp motif in the catalytic core of protein kinases”, Sci. Rep., 5: 10115 (2015).
(7) Benshang Li, Hui Li, Yun Bai, Renate Kirschner-Schwabe, Jun J Yang, Yao Chen, Gang Lu, Gannie Tzoneva, Xiaotu Ma, Tongmin Wu, Wenjing Li, Haisong Lu, Lixia Ding, Huanhuan Liang, Xiaohang Huang, Minjun Yang, Lei Jin, Hui Kang, Shuting Chen, Alicia Du, Shuhong Shen, Jianping Ding, Hongzhuan Chen, Jing Chen, Arend von Stackelberg, Longjun Gu, Jinghui Zhang, Adolfo Ferrando, Jingyan Tang, Shengyue Wang & Bin-Bing S Zhou “Negative feedback–defective PRPS1 mutants drive thiopurine resistance in relapsed childhood ALL”, Nature Med., 21: 563-571 (2015). 
(8) Zhe Zhang$, Shanshan Wang$, Tong Shen, Jiangye Chen, and Jianping Ding* “Crystal structure of the Rab9A-RUTBC2 RBD complex reveals the molecular basis for the binding specificity of Rab9A with RUTBC2”, Structure, 22, 1408-1420 (2014). ($Contributed equally)
(9) Zilong Zhang, Jian Wu, Wei Lin, Jin Wang, Han Yan, Wei Zhao, Jun Ma, Jianping Ding*, Peng Zhang*, and Guoping Zhao* “Subdomain II of a-isopropylmalate synthase is essential for activity: inferring a mechanism of feedback inhibition”, J. Biol. Chem., 289, 27966-27978 (2014).
(10) Shicheng Zhang, Tianlong Zhang, Minghui Yan, Jianping Ding*, and Jiangye Chen* “Crystal structure of the WOPR-DNA complex and implications for Wor1 function in white-opaque switching of Candida albicans”, Cell Res., 24, 1108-1120 (2014).
(11) Zhe Zhang, Tianlong Zhang, Shanshan Wang, Zou Gong, Chun Tang, Jiangye Chen, and Jianping Ding* “Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5”, eLife, 3, e02687 (2014). 
(12) Hui Yang, Tianlong Zhang, Ye Tao, Fang Wang, Liang Tong, and Jianping Ding* “Structural insights into the functions of the FANCM-FAAP24 complex in DNA repair”, Nucleic Acids Res., 41, 10573-10583 (2013).
(13) Shutong Xu, Wenjing Li, Junjun Zhu, Rong Wang, Zheng Li, Guo-Liang Xu, and Jianping Ding* “Crystal structures of isoorotate decarboxylases reveal a novel catalytic mechanism of 5-carboxyl-uracil decarboxylation and shed lights on the search for DNA decarboxylase”, Cell Res., 23, 1296-1309 (2013).  
(14) Jianchuan Wang, Chen Zhong, Fang Wang, Fangfang Qu, and Jianping Ding* “Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif”, Biochem. J., 454, 39-47 (2013).
(15) Ke Xu, Minhua Zhang, Qin Zhao, Fang Yu, Hui Guo, Chengyuan Wang, Fangyuan He, Jianping Ding, and Peng Zhang* “Crystal structure of a folate ECF transporter from Lactobacillus brevis”, Nature, 497, 268-271 (2013).
(16) Wei Huang, Zhen Gong, Jian Li, and Jianping Ding* “Crystal structure of Drosophila melanogaster tryptophan 2,3-dioxygenase reveals insights into substrate recognition and catalytic mechanism”, J. Struct. Biol., 181, 291-299 (2013).
(17) Sisi Li, Jiamu Du, Hui Yang, Juan Yin, Jianping Ding*, and Jiang Zhong* “Functional and structural characterization of DNMT2 from Spodoptera frugiperda”, J. Mol. Cell Biol., 5, 64-66 (2013).
(18) Kuan Hu, Meng Zhao, Tianlong Zhang, Manwu Zha, Chen Zhong, Yu Jiang, and Jianping Ding* “Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutulicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism”, Biochem. J., 449, 79-89 (2013).
(19) Wenjing Li, Chen Zhong, Lei Li, Bingfa Sun, Weiyi Wang, Shutong Xu, Tianlong Zhang, Chunguang Wang, Lan Bao, and Jianping Ding* “Molecular basis of the acetyltransferase activity of MEC-17 towards α-tubulin”, Cell Res., 22, 1707-1711 (2012).
(20) Tianlong Zhang, Marie-Pierre Péli-Gulli, Hui Yang, Claudio De Virgilio, and Jianping Ding* “Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the EGO complex to activate TORC1”, Structure, 20, 2151-2160 (2012).
(21) Manwu Zha, Chen Zhong, Ying Ou, Li Han, Jianchuan Wang, and Jianping Ding* “Crystal structures of human CaMKIa reveal insights into the regulation mechanism of CaMKI”, PLoS One, e44828 (2012).
(22) Hui Yang, Tianlong Zhang, Ye Tao, Lijing Wu, Hong-tao Li, Jin-qiu Zhou, Chen Zhong, and Jianping Ding* “Saccharomyces cerevesiae MHF complex structurally resembles the histones (H3-H4)2 heterotetramer and functions as a heterotetramer”, Structure, 20, 364-370 (2012).
(23) Yufei He, Binzhong Li, Zheng Li, Peng Liu, Yang Wang, Qingyu Tang, Jianping Ding, Yingying Jia, Zhangcheng Chen, Lin Li, Yan Sun, Xiuxue Li, Qing Dai, Chunxiao Song, Kangling Zhang, Chuan He, and Guoliang Xu* “Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA”, Science, 333, 1303-1307 (2011).
(24) Bing Wang, Yingjie Peng, Tianlong Zhang, and Jianping Ding* “Crystal structures and kinetic studies of human kappa class glutathione transferase provide insights into the catalytic mechanism”, Biochem. J., 439, 215-225, (2011).
(25) Bingfa Sun, Shunling Guo, Qingyu Tang, Chen Li, Rong Zeng, Zhiqi Xiong, Chen Zhong, and Jianping Ding* “Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274”, Cell Res., 21, 1262-1266 (2011). (Featured article)
(26) Shutong Xu, Chen Zhong, Tianlong Zhang, and Jianping Ding* “Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd protein”, J. Mol. Cell Biol., 3, 293-300 (2011).
(27) Minyun Zhou, Xianchi Dong, Carsten Baldauf, Hua Chen, Yanfeng Zhou, Timothy A. Springer, Xinping Luo, Chen Zhong, Frauke Gräter, and Jianping Ding* “A novel calcium-binding site of von Willebrand factor A2 domain regulates its cleavage by ADAMTS13”, Blood, 117, 4623-4631 (2011).
(28) Shutong Xu, Jian Wu, Bingfa Sun, Chen Zhong, and Jianping Ding* “Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding”, Nucleic Acids Res., 39, 4438-4449 (2011).
(29) Yuanyuan Chang, Jian Wu, Xiajing Tong, Jinqiu Zhou, and Jianping Ding* “Crystal structure of the catalytic core of Saccharomyces cerevesiae histone demethylase Rph1: insights into the substrate specificity and catalytic mechanism”, Biochem. J., 433, 295-302 (2011).
(30) Bei Yang, Chen Zhong, Yingjie Peng, Zheng Lai, and Jianping Ding* “Molecular mechanisms of “off-on switch” of activities of human IDH1 by tumor-associated mutation R132H”, Cell Res., 20, 1188-1200 (2010).
(31) Hui Yang, Jiamu Du, Jianchuan Wang, Chen Zhong, Dapeng Zhang, Huaizu Guo, Yajun Guo, and Jianping Ding* “Structural basis of the immunosuppressive mechanism of therapeutic antibody daclizumab”, Cell Res., 20, 1361-1371 (2010).
(32) Minyun Zhou, Xianchi Dong, Ning Shen, Chen Zhong, and Jianping Ding* “Crystal structure of Saccaromyces cerevisae tryptophanyl-tRNA synthetase: new insights into the mechanism of tryptophan activation and implications for anti-fungal drug design”, Nucleic Acids Res., 38, 3399-3413 (2010).
(33) Bo Zhou, Shanshan Wang, Luxia Xu, Feilong Meng, Yaoji Xuan, Yimin Duan, Jianyong Wang, Hao Hu, Xianchi Dong, Jianping Ding, and Jinqiu Zhou* “SWR1 complex poises heterochromatin boundaries for anti-silencing activity propagation”, Mol. Cell Biol., 30, 2391-2400 (2010).
(34) Mingliang Zhang, Xiajing Tong, Xiaohong Fu, Bo O Zhou, Jianyong Wang, Xinhua Liao, Qianjin Li, Ning Shen, Jianping Ding, and Jinqiu Zhou* “Yeast telomerase subunit Est1p has guanine quadruplex–promoting activity that is required for telomere elongation”, Nat. Struct. Mol. Biol., 17, 202-209 (2010).
(35) Xianchi Dong, Minyun Zhou, Chen Zhong, Ning Shen, Bei Yang, and Jianping Ding* “Crystal structure of P. Horikoshi tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetases”, Nucleic Acids Res., 38, 1401-1412 (2010).
(36) Jiamu Du, Hui Yang, Dapeng Zhang, Jianchuan Wang, Huaizu Guo, Baozhen Peng, Yajun Guo, and Jianping Ding* “Structural basis for the blockage of IL-2 signaling by therapeutic antibody Basiliximab”, J. Immunol., 184, 1361-1368 (2010). 

 

研究组成员
上海市浦东新区海科路333号,
电话:021-2077 8500
Email: ncpss@sibcb-ncpss.org