Refined Crystal Structure of the Interleukin‐1 Receptor Antagonist
作者： Herman A. Schreuder , Jean Michel Rondeau , Chantal Tardif , Adolfo Soffientini , Edoardo Sarubbi
DOI: 10.1111/J.1432-1033.1995.0838P.X
关键词: Interleukin 1 receptor antagonist 、 Cell biology 、 Crystal structure 、 Stereochemistry 、 Molecular replacement 、 Receptor 、 Protein Data Bank 、 Cytokine 、 Receptor antagonist 、 Antagonist 、 Biology
摘要: Interleukin-I (IL-1) molecules are cytokines involved in the acute-phase response against infection and injury. Three naturally occurring IL-1 known, two agonists: IL-1α IL-1β, one antagonist, 1L-1 receptor antagonist (IL-1ra). Although action protects organism by enhancing to pathogens, its overproduction can lead pathology has been implicated disease states that include septic shock, rheumatoid arthritis, graft versus host certain leukemias. The crystal structure of IL-1ra solved at 0.21-nm resolution molecular replacement using IL-1β as a search model. crystals contain independent which very similar, same fold IL-1β. consists twelve β-strands form six-stranded β-barrel, closed on side three β-hairpin loops. Cys69 Cys116 linked via disulfide bond Pro53 built cisconformation. Comparison with structures present Protein Data Bank shows putative interaction region, involving N-terminus up beginning strand β1 loops D G, is different molecules. Other regions, identified mutagenesis studies, structurally conserved rigid, allowing precise specific interactions receptor.
sci-hub.se 参考文章(62)
Nancy P Camacho, Deborah R Smith, Adrian Goldman, Bohdan Schneider, David Green, Peter R Young, Helen M Berman, None, Structure of an interleukin-1 beta mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition. Biochemistry. ,vol. 32, pp. 8749- 8757 ,(1993) , 10.1021/BI00085A005
G. Ju, E. Labriola-Tompkins, C. A. Campen, W. R. Benjamin, J. Karas, J. Plocinski, D. Biondi, K. L. Kaffka, P. L. Kilian, S. P. Eisenberg, Conversion of the interleukin 1 receptor antagonist into an agonist by site-specific mutagenesis. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 88, pp. 2658- 2662 ,(1991) , 10.1073/PNAS.88.7.2658
Brian J. Stockman, Terrence A. Scahill, Melinda Roy, Eldon L. Ulrich, Nancy A. Strakalaitis, David P. Brunner, Anthony W. Yem, Martin R. Deibel, Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy. Biochemistry. ,vol. 31, pp. 5237- 5245 ,(1992) , 10.1021/BI00138A001
Kjell Ohlsson, Peter Björk, Magnus Bergenfeldt, Robert Hageman, Robert C. Thompson, Interleukin-1 receptor antagonist reduces mortality from endotoxin shock. Nature. ,vol. 348, pp. 550- 552 ,(1990) , 10.1038/348550A0
Paul Wingfield, Pierre Graber, N.Rao Movva, Angela M. Gronenborn, H.Robson MacDonald, N-terminal-methionylated interleukin-1β has reduced receptor-binding affinity FEBS Letters. ,vol. 215, pp. 160- 164 ,(1987) , 10.1016/0014-5793(87)80133-3
Bradford J. Graves, Marcos H. Hatada, Wayne A. Hendrickson, Julann K. Miller, Vincent S. Madison, Yoshinori Satow, Structure of interleukin 1 alpha at 2.7-A resolution. Biochemistry. ,vol. 29, pp. 2679- 2684 ,(1990) , 10.1021/BI00463A009
J. Habazettl, D. Gondol, R. Wiltscheck, J. Otlewski, M. Schleicher, T. A. Holak, Structure of hisactophilin is similar to interleukin-1|[beta]| and fibroblast growth factor Nature. ,vol. 359, pp. 855- 858 ,(1994) , 10.1038/359855A0
Sandra M. Zurawski, Karl Pope, Holly Cherwinski, Gerard Zurawski, Expression in Escherichia coli of synthetic human interleukin-1α genes encoding the processed active protein, mutant proteins, and β-galactosidase fusion proteins Gene. ,vol. 49, pp. 61- 68 ,(1986) , 10.1016/0378-1119(86)90385-9
A. J. Howard, G. L. Gilliland, B. C. Finzel, T. L. Poulos, D. H. Ohlendorf, F. R. Salemme, The use of an imaging proportional counter in macromolecular crystallography Journal of Applied Crystallography. ,vol. 20, pp. 383- 387 ,(1987) , 10.1107/S0021889887086436
Brian Henderson, Simon Blake, Therapeutic potential of cytokine manipulation. Trends in Pharmacological Sciences. ,vol. 13, pp. 145- 152 ,(1992) , 10.1016/0165-6147(92)90052-8