苏晓东
X射线蛋白晶体学,蛋白质化学,酶学,分子生物学,药物设计,蛋白质工程。
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- 姓名:苏晓东
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博士生导师
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学科领域:
光学
- 研究兴趣:X射线蛋白晶体学,蛋白质化学,酶学,分子生物学,药物设计,蛋白质工程。
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苏晓东
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苏晓东
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苏晓东
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苏晓东
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【期刊论文】The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
苏晓东, Xiao-Dong Su, *, Nlccolo' Taddel †, Masslmo Stefanl †, Glampletro Ramponl† & Par Nordlund *
NATURE,-0001,():
-1年11月30日
PROTEIN tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development1. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase)2, a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates3-6, and overexpression of the protein in nor-mal and transformed cells inhibits cell proliferation7,8. The structure of the low-molecular-weight PTPase reveals an a/β protein containing a phosphate-binding loop motif at the amino end of helix al. This motif includes the essential active-site residues Cys 12 and Arg 18 and bears striking similarities to the activesite motif recently described in the structure of human PTP1B9. The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism. The structure also suggests a catalytic role for Asp 129 in the reaction cycle.
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【期刊论文】Structural genomics efforts at the Chinese Academy of Sciences and Peking University
苏晓东, W.M. Gong, H.Y. Liu, L.W. Niu, Y.Y. Shi, *, Y.J. Tang, M.K. Teng, J.H. Wu, D.C. Liang, D.C. Wang, J.F. Wang, J.P. Ding, H.Y. Hu, Q.H. Huang, Q.H. Zhang, S.Y. Lu, J.L. An, Y.H. Liang, X.F. Zheng, X.C. Gu & X.D. Su
Journal of Structural and Functional Genomics 4: 137-139, 2003.,-0001,():
-1年11月30日
Structural genomics efforts at the Chinese Academy of Sciences and Peking University are reported in this article. The major targets for the structural genomics project are targeted proteins expressed in human hematopoietic stem/progenitor cells, proteins related to blood diseases and other human proteins. Up to now 328 target genes have been constructed in expression vectors. Among them, more than 50% genes have been expressed in Escherichia coli, approximately 25% of the resulting proteins are soluble, and 35 proteins have been purified. Crystallization, data collection and structure determination are continuing. Experiences accumulated during this initial stage are useful for designing and applying high-throughput approaches in structural genomics.
blood disease,, hematopoietic stem/, progenitor cells,, nuclear magnetic resonance,, protein structure,, structural genomics,, X-ray rystallography
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苏晓东, Delin You, a Qiang Chen, a Yuhe Liang, a Jianli An, a Rui Li, a Xiaocheng Gu, a Ming Luoa, b and Xiao-Dong Sua *
Acta Cryst. (2003). D59, 1863-1865,-0001,():
-1年11月30日
Native and His-tagged mutant (L160I) hypoxanthine-guanine phosphoribosyltransferase (HGPRT) from Thermoanaerobacter tengcongensis were cloned, expressed in Escherichia coli and purified. Both proteins were crystallized with polyethylene glycol as the main precipitant at 293 Kusing the hanging-drop vapour-diffusion method. The crystal of native HGPRT belongs to space group C2221, with unit-cell parameters a=65.77, b=137.73, c=95.27 A
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【期刊论文】Crystal Structure of Hemolin: A Horseshoe Shape with Implications for Homophilic Adhesion
苏晓东, Xiao-Dong Su, * Louis N. Gastinel, † Daniel E. Vaughn, ‡ Ingrid Faye, Pak Poon, Pamela J. Bjorkman §
SCIENCE VOL 281 14 AUGUST 1998,-0001,():
-1年11月30日
Hemolin, an insect immunoglobulin superfamily member, is a lipopolysaccharide-binding immune protein induced during bacterial infection. The 3.1 angstrom crystal structure reveals a bound phosphate and patches of positive charge, which may represent the lipopolysaccharide binding site, and a new and unexpected arrangement of four immunoglobulin-like domains forming a horseshoe. Sequence analysis and analytical ultracentrifugation suggest that the domain arrangement is a feature of the L1 family of neural cell adhesion molecules related to hemolin. These results are relevant to interpretation of human L1 mutations in neurological diseases and suggest a domain swapping model for how L1 family proteins mediate homophilic adhesion.
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