Crystallization and preliminary X-ray diffraction analysis of the two distinct types of zebrafish β2-microglobulin.

作者: Zhaosan Chen , Nianzhi Zhang , Shuangshuang Lu , Mansoor Tariq , Junya Wang

DOI: 10.1107/S2053230X15005737

关键词:

摘要: β(2)-Microglobulin (β(2)m) noncovalently associates with the heavy chain of major histocompatibility complex class I (MHC I) molecules, which bind foreign antigen peptides to control cytotoxic T lymphocyte (CTL) immune response. In contrast mammals, there are distinct types β(2)ms derived from two loci in a number teleost species. order clarify structures β(2)ms, zebrafish (Danio rerio) Dare-β(2)m-I and Dare-β(2)m-II were expressed Escherichia coli, purified crystallized, diffraction data collected 1.6 1.9 A resolution, respectively. Both crystals belonged space group P2(1)2(1)2(1). The unit-cell parameters determined be = 38.2, b 50.4, c 50.9 for 38.9, 52.7, 65.8 Dare-β(2)m-II. Each asymmetric unit was constituted one molecule, Matthews coefficients 2.22 3.01 A(3) Da(-1) solvent contents 45 59% Dare-β(2)m-II, These β(2)m will provide relevant information further studies MHC complex.

参考文章(13)
Jianhua Zhang, Yong Chen, Jianxun Qi, Feng Gao, Yanjie Liu, Jun Liu, Xuyu Zhou, Jim Kaufman, Chun Xia, George F. Gao, Narrow Groove and Restricted Anchors of MHC Class I Molecule BF2*0401 Plus Peptide Transporter Restriction Can Explain Disease Susceptibility of B4 Chickens Journal of Immunology. ,vol. 189, pp. 4478- 4487 ,(2012) , 10.4049/JIMMUNOL.1200885
Katharine E. Magor, Benny P. Shum, Peter Parham, The β2-Microglobulin Locus of Rainbow Trout (Oncorhynchus mykiss) Contains Three Polymorphic Genes The Journal of Immunology. ,vol. 172, pp. 3635- 3643 ,(2004) , 10.4049/JIMMUNOL.172.6.3635
Zbyszek Otwinowski, Wladek Minor, Processing of X-ray diffraction data collected in oscillation mode Methods in Enzymology. ,vol. 276, pp. 307- 326 ,(1997) , 10.1016/S0076-6879(97)76066-X
Mats L. Lundqvist, Paulina Appelkvist, Trudi Hermsen, Lars Pilström, René J. M. Stet, Characterization of beta2-microglobulin in a primitive fish, the Siberian sturgeon (Acipenser baeri). Immunogenetics. ,vol. 50, pp. 79- 83 ,(1999) , 10.1007/S002510050690
Rong Chen, Jianxun Qi, Shugang Yao, Xiaocheng Pan, Feng Gao, Chun Xia, Expression, crystallization and preliminary crystallographic analysis of C-reactive protein from zebrafish. Acta Crystallographica Section F-structural Biology and Crystallization Communications. ,vol. 67, pp. 1633- 1636 ,(2011) , 10.1107/S1744309111037390
J. W. Becker, G. N. Reeke, Three-dimensional structure of beta 2-microglobulin Proceedings of the National Academy of Sciences of the United States of America. ,vol. 82, pp. 4225- 4229 ,(1985) , 10.1073/PNAS.82.12.4225
Bo Jiang, Yanjie Liu, Rong Chen, Zhenbao Wang, Mansoor Tariq, Chun Xia, Crystallization and preliminary X-ray diffraction analysis of a single variable domain of the immunoglobulin superfamily in amphioxus, Amphi-IgSF-V. Acta Crystallographica Section F-structural Biology and Crystallization Communications. ,vol. 70, pp. 1072- 1075 ,(2014) , 10.1107/S2053230X14012746
Hui-Fang Hao, Tian-Yao Yang, Ruo-Qian Yan, Feng-Shan Gao, Chun Xia, cDNA cloning and genomic structure of grass carp (Ctenophayngodon idellus) beta2-microglobulin gene. Fish & Shellfish Immunology. ,vol. 20, pp. 118- 123 ,(2006) , 10.1016/J.FSI.2005.04.003
Shuangshuang Lu, Shugang Yao, Rong Chen, Nianzhi Zhang, Jianmin Chen, Feng Gao, Chun Xia, Expression, purification, crystallization and preliminary X-ray diffraction analysis of nurse shark β2-microglobulin. Acta Crystallographica Section F-structural Biology and Crystallization Communications. ,vol. 68, pp. 460- 463 ,(2012) , 10.1107/S1744309112006811
Weihong Chen, Feng Gao, Fuliang Chu, Jianhua Zhang, George F. Gao, Chun Xia, Crystal Structure of a Bony Fish β2-Microglobulin INSIGHTS INTO THE EVOLUTIONARY ORIGIN OF IMMUNOGLOBULIN SUPERFAMILY CONSTANT MOLECULES Journal of Biological Chemistry. ,vol. 285, pp. 22505- 22512 ,(2010) , 10.1074/JBC.M109.095000