Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the human TLE1 Q domain  

作　　者：Su Wang Jiamu Du Hua Tang Xinyu Ding Manwu Zha Zhifei Xu 

机构地区：[1]Department of Thoracic and Cardiovascular Surgery, Changzheng Hospital, Second Military Medical University, Shanghai 200003, China [2]Research Center for Structural Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China [3]Present address: Memorial Sloan-Kettering Cancer Center, NY 10021, USA

出　　处：《Acta Biochimica et Biophysica Sinica》2011年第2期149-153,共5页生物化学与生物物理学报（英文版）

基　　金：Acknowledgements We thank Prof. Jianping Ding at Institute of Biochemistry and Cell Biology （SIBCB）, Shanghai Institutes for Biological Sciences （SIBS）, Chinese Academy of Sciences （CAS） for the guidance of the project. We are grateful to the staff members at the Shanghai Synchrotron Radiation Facility and the Research Center for Structural Biology of SIBCB, SIBS, CAS for technical supports in diffraction data collection and helpful discussion.This work was supported by the National Natural Science Foundation of China （30972965 and 30800171） and the State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.

摘　　要：Human transducin-like enhancer of split 1 （TLE1） plays crucial roles in a number of developmental processes and is involved in pathogenesis of malignancy tumors. The N-terminal glutamine-rich domain （Q domain） of TLE1 mediates its tetramerization and interactions with different DNA-binding transcription factors to regulate Notch and Wnt signaling pathways. To better understand the molecular mechanism of TLE1＇s functions in these pathways, we cloned, purified, and crystallized the TLE1 Q domain （TLE1-Q）. The crystals belong to space group C2221, with the complete diffraction data of the native and Se-Met TLE1-Q collected to 3.5 and 4.1A resol- utions, respectively. The phasing-solving and model build- ing are in progress.Human transducin-like enhancer of split 1 （TLE1） plays crucial roles in a number of developmental processes and is involved in pathogenesis of malignancy tumors. The N-terminal glutamine-rich domain （Q domain） of TLE1 mediates its tetramerization and interactions with different DNA-binding transcription factors to regulate Notch and Wnt signaling pathways. To better understand the molecular mechanism of TLE1＇s functions in these pathways, we cloned, purified, and crystallized the TLE1 Q domain （TLE1-Q）. The crystals belong to space group C2221, with the complete diffraction data of the native and Se-Met TLE1-Q collected to 3.5 and 4.1A resol- utions, respectively. The phasing-solving and model build- ing are in progress.

关 键 词：CRYSTALLIZATION GLUTAMINE LEF1 NOTCH SELENOMETHIONINE TLE1 X-ray prokaryotic expression 

分 类 号：Q51[生物学—生物化学] TQ463.6[化学工程—制药化工]