Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
권호 표지
DOI QR코드

DOI QR Code

X-ray Crystallographic Structure of TIR-Domain from the Human TIR-Domain Containing Adaptor Protein/MyD88-Adaptor-Like Protein (TIRAP/MAL)

  • Woo, Ju-Rang (Joslin Diabetes Center & Department of Medicine, Harvard Medical School) ;
  • Kim, Sun-Min (School of Systems Biomedical Science, Soongsil University) ;
  • Shoelson, Steven E. (Joslin Diabetes Center & Department of Medicine, Harvard Medical School) ;
  • Park, Sang-Youn (School of Systems Biomedical Science, Soongsil University)
  • Received : 2012.05.08
  • Accepted : 2012.05.31
  • Published : 2012.09.20
Download PDF
⟨ Previous Next ⟩

Abstract

Keywords

References

  1. O'Neill, L. A.; Fitzgerald, K. A.; Bowie, A. G. Trends Immunol. 2003, 24, 286-290. https://doi.org/10.1016/S1471-4906(03)00115-7
  2. Yamamoto, M.; Takeda, K.; Akira, S. Mol. Immunol. 2004, 40, 861-868. https://doi.org/10.1016/j.molimm.2003.10.006
  3. Xu, Y.; Tao, X.; Shen, B.; Horng, T.; Medzhitov, R.; Manley, J. L.; Tong, L. Nature 2000, 408, 111-115. https://doi.org/10.1038/35040600
  4. Nyman, T.; Stenmark, P.; Flodin, S.; Johansson, I.; Hammarstrom, M.; Nordlund, P. J. Biol. Chem. 2008, 283, 11861-11865. https://doi.org/10.1074/jbc.C800001200
  5. Khan, J. A.; Brint, E. K.; O'Neill, L. A.; Tong, L. J. Biol. Chem. 2004, 279, 31664-31670. https://doi.org/10.1074/jbc.M403434200
  6. Ohnishi, H.; Tochio, H.; Kato, Z.; Orii, K. E.; Li, A., Kimura, T.; Hiroaki, H.; Kondo, N.; Shirakawa, M. Proc. Natl. Acad Sci. U S A. 2009, 106, 10260-10265. https://doi.org/10.1073/pnas.0812956106
  7. Chan, S. L.; Low, L. Y.; Hsu, S.; Li, S.; Liu, T.; Santelli, E.; Le Negrate, G.; Reed, J. C.; Woods, V. L., Jr.; Pascual, J. J. Biol. Chem. 2009, 284, 21386-21392. https://doi.org/10.1074/jbc.C109.007591
  8. Chan, S. L.; Mukasa, T.; Santelli, E.; Low, L. Y.; Pascual, J. Protein Sci. 2010, 19, 155-161.
  9. Fitzgerald, K. A.; Palsson-McDermott, E. M.; Bowie, A. G.; Jefferies, C. A.; Mansell, A. S.; Brady, G.; Brint, E.; Dunne, A.; Gray, P.; Harte, M. T.; McMurray, D.; Smith, D. E.; Sims, J. E.; Bird, T. A.; O'Neill, L. A. J. Nature 2001, 413, 78-83. https://doi.org/10.1038/35092578
  10. Horng, T.; Barton, G. M.; Medzhitov, R. Nature Immun. 2001, 2, 835-841. https://doi.org/10.1038/ni0901-835
  11. Horng, T.; Barton, G. M.; Flavell, R. A.; Medzhitov, R. Nature 2002, 420, 329-333. https://doi.org/10.1038/nature01180
  12. Kagan, J. C.; Medzhitov, R. Cell 2006, 125, 943-955. https://doi.org/10.1016/j.cell.2006.03.047
  13. Khor, C. C.; Chapman, S. J.; Vannberg, F. O.; Dunne, A.; Murphy, C.; Ling, E. Y.; Frodsham, A. J.; Walley, A. J.; Kyrieleis, O.; Khan, A.; Aucan, C.; Segal, S. Nature Genet. 2007, 39, 523-528. https://doi.org/10.1038/ng1976
  14. Nejentsev, S.; Thye, T.; Szeszko, J. S.; Stevens, H.; Balabanova, Y.; Chinbuah, A. M.; Hibberd, M.; van de Vosse, E.; Alisjahbana, B.; van Crevel, R.; Ottenhoff, T. H. M.; Png, E.; Drobniewski, F.; Todd, J. A.; Seielstad, M.; Horstmann, R. D. Nature Genet. 2008, 40, 261-262. https://doi.org/10.1038/ng0308-261
  15. George, J.; Kubarenko, A. V.; Rautanen, A.; Mills, T. C.; Colak, E.; Kempf, T.; Hill, A. V. S.; Nieters, A.; Weber, A. N. R. J. Immun. 2010, 184, 3025-3032. https://doi.org/10.4049/jimmunol.0901156
  16. Valkov, E.; Stamp, A.; Dimaio, F.; Baker, D.; Verstak, B.; Roversi, P.; Kellie, S.; Sweet, M. J.; Mansell, A.; Gay, N. J.; Martin, J. L.; Kobe, B. Proc. Natl. Acad Sci. U S A. 2011, 108, 14879-14884. https://doi.org/10.1073/pnas.1104780108
  17. Otwinowski, Z.; Minor, W. Methods Enzymol. 1997, 276, 307- 325. https://doi.org/10.1016/S0076-6879(97)76066-X
  18. Matthews, B. W. J. Mol. Biol. 1968, 33, 491-497. https://doi.org/10.1016/0022-2836(68)90205-2
  19. McCoy, A. J.; Grosse-Kunstleve, R. W.; Storoni, L. C.; Read, R. J. Acta Cryst. 2005, D61, 458-464.
  20. Vagin, A. A.; Steiner, R. S.; Lebedev, A. A.; Potterton, L.; McNicholas, S.; Long, F.; Murshudov, G. N. Acta Cryst. 2004, D60, 2284-2295.
  21. Emsley, P.; Cowtan, K. Acta Crystallogr. D Biol. Crystallogr. 2004, 60, 2126-2132. https://doi.org/10.1107/S0907444904019158
  22. Brunger, A. T.; Adams, P. D.; Clore, G. M.; DeLano, W. L.; Gros P.; Grosse-Kunstleve, R. W.; Jiang, J. S.; Kuszewski, J.; Nilges, M.; Pannu, N. S.; Read, R. J.; Rice, L. M.; Simonson, T.; Warren, G. L. Acta Crystallogr. D Biol. Crystallogr. 1998, 54, 905-921. https://doi.org/10.1107/S0907444998003254
  23. DeLano, W. L. The PyMOL Molecular Graphics System; DeLano Scientific: San Carlos, CA, USA. 2002.
  24. Krissinel, E.; Henrick, K. J. Mol. Biol. 2007, 372, 774-797. https://doi.org/10.1016/j.jmb.2007.05.022
  25. Ponstingl, H.; Henrick, K.; Thornton, J. M. Proteins 2000, 41, 47- 57. https://doi.org/10.1002/1097-0134(20001001)41:1<47::AID-PROT80>3.0.CO;2-8
  26. Shoemaker, B. A.; Panchenko, A. R.; Bryant, S. H. Protein Sci. 2006, 15, 352-361. https://doi.org/10.1110/ps.051760806

Cited by

  1. Solution structure of the TLR adaptor MAL/TIRAP reveals an intact BB loop and supports MAL Cys91 glutathionylation for signaling vol.114, pp.32, 2017, https://doi.org/10.1073/pnas.1701868114
  2. A non-uniform sampling approach enables studies of dilute and unstable proteins vol.68, pp.2, 2017, https://doi.org/10.1007/s10858-017-0091-z
  3. A Comparative Analysis of the Mechanism of Toll-Like Receptor-Disruption by TIR-Containing Protein C from Uropathogenic Escherichia coli vol.5, pp.1, 2016, https://doi.org/10.3390/pathogens5010025
  4. Insight into Phosphatidylinositol-Dependent Membrane Localization of the Innate Immune Adaptor Protein Toll/Interleukin 1 Receptor Domain-Containing Adaptor Protein vol.9, pp.1664-3224, 2018, https://doi.org/10.3389/fimmu.2018.00075