메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

The structural basis for receptor recognition of human interleukin-18

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 18; INTERLEUKIN 18 RECEPTOR; INTERLEUKIN 18 RECEPTOR ALPHA; INTERLEUKIN 18 RECEPTOR BETA; INTERLEUKIN 1BETA; PHENYLALANINE; IL1RAP PROTEIN, HUMAN; INTERLEUKIN 1 RECEPTOR ACCESSORY PROTEIN; INTERLEUKIN 18 PROTEIN, HUMAN; INTERLEUKIN RECEPTOR; INTERLEUKIN-36 RECEPTOR, HUMAN; PROTEIN BINDING; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

EID: 84923278457     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6340     Document Type: Article
Times cited : (98)

References (55)
  • 1
    • 0028845730 scopus 로고
    • Cloning of a new cytokine that induces IFN-gamma production by T cells
    • Okamura, H. et al. Cloning of a new cytokine that induces IFN-gamma production by T cells. Nature 378, 88-91 (1995).
    • (1995) Nature , vol.378 , pp. 88-91
    • Okamura, H.1
  • 2
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme
    • Kuida, K. et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science 267, 2000-2003 (1995).
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1
  • 3
    • 0028984948 scopus 로고
    • Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock
    • Li, P. et al. Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock. Cell 80, 401-411 (1995).
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1
  • 4
    • 0031004174 scopus 로고    scopus 로고
    • Caspase-1 processes IFN-gamma-inducing factor and regulates LPS-induced IFN-gamma production
    • Ghayur, T. et al. Caspase-1 processes IFN-gamma-inducing factor and regulates LPS-induced IFN-gamma production. Nature 386, 619-623 (1997).
    • (1997) Nature , vol.386 , pp. 619-623
    • Ghayur, T.1
  • 6
    • 84862006672 scopus 로고    scopus 로고
    • TRAM is involved in IL-18 signaling and functions as a sorting adaptor for MyD88
    • Ohnishi, H. et al. TRAM is involved in IL-18 signaling and functions as a sorting adaptor for MyD88. PLoS ONE 7, e38423 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e38423
    • Ohnishi, H.1
  • 7
    • 0032127279 scopus 로고    scopus 로고
    • Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function
    • Adachi, O. et al. Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function. Immunity 9, 143-150 (1998).
    • (1998) Immunity , vol.9 , pp. 143-150
    • Adachi, O.1
  • 8
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A. & Kolodner, R. D. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 29, 301-305 (2001).
    • (2001) Nat. Genet. , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 9
  • 10
    • 84864545087 scopus 로고    scopus 로고
    • Treating inflammation by blocking interleukin-1 in a broad spectrum of diseases
    • Dinarello, C. a., Simon, A. & van der Meer, J. W. M. Treating inflammation by blocking interleukin-1 in a broad spectrum of diseases. Nat. Rev. Drug Discov. 11, 633-652 (2012).
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 633-652
    • Dinarello, C.A.1    Simon, A.2    Van Der Meer, J.W.M.3
  • 12
    • 79959963298 scopus 로고    scopus 로고
    • Pathogenesis of systemic juvenile idiopathic arthritis: Some answers, more questions
    • Mellins, E. D., Macaubas, C. & Grom, A. A. Pathogenesis of systemic juvenile idiopathic arthritis: some answers, more questions. Nat. Rev. Rheumatol. 7, 416-426 (2011).
    • (2011) Nat. Rev. Rheumatol. , vol.7 , pp. 416-426
    • Mellins, E.D.1    Macaubas, C.2    Grom, A.A.3
  • 13
    • 84868195423 scopus 로고    scopus 로고
    • Genome-wide association study identifies eight new susceptibility loci for atopic dermatitis in the Japanese population
    • Hirota, T. et al. Genome-wide association study identifies eight new susceptibility loci for atopic dermatitis in the Japanese population. Nat. Genet. 44, 1222-1226 (2012).
    • (2012) Nat. Genet. , vol.44 , pp. 1222-1226
    • Hirota, T.1
  • 15
    • 84922008927 scopus 로고    scopus 로고
    • Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation
    • Romberg, N. et al. Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation. Nat. Genet. 46, 1135-1139 (2014).
    • (2014) Nat. Genet. , vol.46 , pp. 1135-1139
    • Romberg, N.1
  • 16
    • 84927126118 scopus 로고    scopus 로고
    • An activating NLRC4 inflammasome mutation causes autoinflammation with recurrent macrophage activation syndrome
    • Canna, S. W. et al. An activating NLRC4 inflammasome mutation causes autoinflammation with recurrent macrophage activation syndrome. Nat. Genet. 46, 1140-1146 (2014).
    • (2014) Nat. Genet. , vol.46 , pp. 1140-1146
    • Canna, S.W.1
  • 17
    • 33745026413 scopus 로고    scopus 로고
    • Contribution of IL-18 to atopic-dermatitis-like skin inflammation induced by Staphylococcus aureus product in mice
    • Terada, M. et al. Contribution of IL-18 to atopic-dermatitis-like skin inflammation induced by Staphylococcus aureus product in mice. Proc. Natl Acad. Sci. USA 103, 8816-8821 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8816-8821
    • Terada, M.1
  • 18
    • 84887430028 scopus 로고    scopus 로고
    • Divergence of IL-1, IL-18, and cell death in NLRP3 inflammasomopathies
    • Brydges, S. D. et al. Divergence of IL-1, IL-18, and cell death in NLRP3 inflammasomopathies. J. Clin. Invest. 123, 4695-4705 (2013).
    • (2013) J. Clin. Invest. , vol.123 , pp. 4695-4705
    • Brydges, S.D.1
  • 19
    • 0242407130 scopus 로고    scopus 로고
    • The structure and binding mode of interleukin-18
    • Kato, Z. et al. The structure and binding mode of interleukin-18. Nat. Struct. Biol. 10, 966-971 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 966-971
    • Kato, Z.1
  • 20
    • 58549098246 scopus 로고    scopus 로고
    • Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein
    • Krumm, B., Meng, X., Li, Y., Xiang, Y. & Deng, J. Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein. Proc. Natl Acad. Sci. USA 105, 20711-20715 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20711-20715
    • Krumm, B.1    Meng, X.2    Li, Y.3    Xiang, Y.4    Deng, J.5
  • 21
    • 69949161901 scopus 로고    scopus 로고
    • Unusual water-mediated antigenic recognition of the proinflammatory cytokine interleukin-18
    • Argiriadi, M. A., Xiang, T., Wu, C., Ghayur, T. & Borhani, D. W. Unusual water-mediated antigenic recognition of the proinflammatory cytokine interleukin-18. J. Biol. Chem. 284, 24478-24489 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 24478-24489
    • Argiriadi, M.A.1    Xiang, T.2    Wu, C.3    Ghayur, T.4    Borhani, D.W.5
  • 22
    • 84866153540 scopus 로고    scopus 로고
    • A unique bivalent binding and inhibition mechanism by the yatapoxvirus interleukin 18 binding protein
    • Krumm, B., Meng, X.,Wang, Z., Xiang, Y. & Deng, J. A unique bivalent binding and inhibition mechanism by the yatapoxvirus interleukin 18 binding protein. PLoS Pathog. 8, e1002876 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1002876
    • Krumm, B.1    Meng, X.2    Wang, Z.3    Xiang, Y.4    Deng, J.5
  • 23
    • 77956950823 scopus 로고    scopus 로고
    • Structural insights into the assembly and activation of IL-1β with its receptors
    • Wang, D. et al. Structural insights into the assembly and activation of IL-1β with its receptors. Nat. Immunol. 11, 905-911 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 905-911
    • Wang, D.1
  • 24
    • 84861307007 scopus 로고    scopus 로고
    • Structure of the activating IL-1 receptor signaling complex
    • Thomas, C., Bazan, J. F. & Garcia, K. C. Structure of the activating IL-1 receptor signaling complex. Nat. Struct. Mol. Biol. 19, 455-457 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 455-457
    • Thomas, C.1    Bazan, J.F.2    Garcia, K.C.3
  • 25
    • 84883815093 scopus 로고    scopus 로고
    • Structural insights into the interaction of IL-33 with its receptors
    • Liu, X. et al. Structural insights into the interaction of IL-33 with its receptors. Proc. Natl. Acad. Sci. USA 110, 14918-14923 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 14918-14923
    • Liu, X.1
  • 26
    • 0030998098 scopus 로고    scopus 로고
    • Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta
    • Vigers, G. P., Anderson, L. J., Caffes, P. & Brandhuber, B. J. Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta. Nature 386, 190-194 (1997).
    • (1997) Nature , vol.386 , pp. 190-194
    • Vigers, G.P.1    Anderson, L.J.2    Caffes, P.3    Brandhuber, B.J.4
  • 27
    • 84904264198 scopus 로고    scopus 로고
    • Molecular determinants of agonist and antagonist signaling through the IL-36 receptor
    • Günther, S. & Sundberg, E. J. Molecular determinants of agonist and antagonist signaling through the IL-36 receptor. J. Immunol. 193, 921-930 (2014).
    • (2014) J. Immunol. , vol.193 , pp. 921-930
    • Günther, S.1    Sundberg, E.J.2
  • 28
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein-protein complexes
    • Takahashi, H., Nakanishi, T., Kami, K., Arata, Y. & Shimada, I. A novel NMR method for determining the interfaces of large protein-protein complexes. Nat. Struct. Biol. 7, 220-223 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 29
    • 84890235827 scopus 로고    scopus 로고
    • The interleukin-1 family: Back to the future
    • Garlanda, C., Dinarello, C. a. & Mantovani, A. The interleukin-1 family: back to the future. Immunity 39, 1003-1018 (2013).
    • (2013) Immunity , vol.39 , pp. 1003-1018
    • Garlanda, C.1    Dinarello, C.A.2    Mantovani, A.3
  • 30
    • 57349124885 scopus 로고    scopus 로고
    • Human IgG1 expression in silkworm larval hemolymph using BmNPV bacmids and its N-linked glycan structure
    • Park, E. Y. et al. Human IgG1 expression in silkworm larval hemolymph using BmNPV bacmids and its N-linked glycan structure. J. Biotechnol. 139, 108-114 (2009).
    • (2009) J. Biotechnol. , vol.139 , pp. 108-114
    • Park, E.Y.1
  • 31
    • 77958149102 scopus 로고    scopus 로고
    • IL-37 is a fundamental inhibitor of innate immunity
    • Nold, M. F. et al. IL-37 is a fundamental inhibitor of innate immunity. Nat. Immunol. 11, 1014-1022 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 1014-1022
    • Nold, M.F.1
  • 32
    • 0036020218 scopus 로고    scopus 로고
    • Interleukin-1F7B (IL-1H4/IL-1F7) is processed by caspase-1 and mature IL-1F7B binds to the IL-18 receptor but does not induce IFN-gamma production
    • Kumar, S. et al. Interleukin-1F7B (IL-1H4/IL-1F7) is processed by caspase-1 and mature IL-1F7B binds to the IL-18 receptor but does not induce IFN-gamma production. Cytokine 18, 61-71 (2002).
    • (2002) Cytokine , vol.18 , pp. 61-71
    • Kumar, S.1
  • 33
    • 28244497331 scopus 로고    scopus 로고
    • Human anti-human IL-18 antibody recognizing the IL-18-binding site 3 with IL-18 signaling blocking activity
    • Hamasaki, T. et al. Human anti-human IL-18 antibody recognizing the IL-18-binding site 3 with IL-18 signaling blocking activity. J. Biochem. 138, 433-442 (2005).
    • (2005) J. Biochem. , vol.138 , pp. 433-442
    • Hamasaki, T.1
  • 34
    • 0035853034 scopus 로고    scopus 로고
    • Site-specific mutations in the mature form of human IL-18 with enhanced biological activity and decreased neutralization by IL-18 binding protein
    • Kim, S. H. et al. Site-specific mutations in the mature form of human IL-18 with enhanced biological activity and decreased neutralization by IL-18 binding protein. Proc. Natl Acad. Sci. USA 98, 3304-3309 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3304-3309
    • Kim, S.H.1
  • 35
    • 84921767532 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray crystallographic analysis of human IL-18 and its extracellular complexes
    • Kimura, T. et al. Purification, crystallization and preliminary X-ray crystallographic analysis of human IL-18 and its extracellular complexes. Acta Crystallogr. Sect. F, Struct. Biol. Commun. 70, 1351-1356 (2014).
    • (2014) Acta Crystallogr. Sect. F, Struct. Biol. Commun. , vol.70 , pp. 1351-1356
    • Kimura, T.1
  • 36
    • 10444256348 scopus 로고    scopus 로고
    • Efficient large-scale protein production of larvae and pupae of silkworm by Bombyx mori nuclear polyhedrosis virus bacmid system
    • Motohashi, T., Shimojima, T., Fukagawa, T., Maenaka, K. & Park, E. Y. Efficient large-scale protein production of larvae and pupae of silkworm by Bombyx mori nuclear polyhedrosis virus bacmid system. Biochem. Biophys. Res. Commun. 326, 564-569 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 564-569
    • Motohashi, T.1    Shimojima, T.2    Fukagawa, T.3    Maenaka, K.4    Park, E.Y.5
  • 37
    • 84923278969 scopus 로고    scopus 로고
    • Silkworm baculovirus expression system for molecular medicine
    • Kajikawa, M. et al. Silkworm Baculovirus Expression System for Molecular Medicine. J. Biotechnol. Biomater. S9, 1-5 (2012).
    • (2012) J. Biotechnol. Biomater. , vol.S9 , pp. 1-5
    • Kajikawa, M.1
  • 40
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: Space-group determination, scaling and intensity statistics
    • Evans, P. R. An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr. D. Biol. Crystallogr. 67, 282-292 (2011).
    • (2011) Acta Crystallogr. D. Biol. Crystallogr. , vol.67 , pp. 282-292
    • Evans, P.R.1
  • 41
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 42
    • 0036901176 scopus 로고    scopus 로고
    • Statistical density modification with non-crystallographic symmetry
    • Terwilliger, T. C. Statistical density modification with non-crystallographic symmetry. Acta Crystallogr. D. Biol. Crystallogr. 58, 2082-2086 (2002).
    • (2002) Acta Crystallogr. D. Biol. Crystallogr. , vol.58 , pp. 2082-2086
    • Terwilliger, T.C.1
  • 45
    • 84860287260 scopus 로고    scopus 로고
    • Exploiting structure similarity in refinement: Automated NCS and target-structure restraints in BUSTER
    • Smart, O. S. et al. Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER. Acta Crystallogr. D. Biol. Crystallogr. 68, 368-380 (2012).
    • (2012) Acta Crystallogr. D. Biol. Crystallogr. , vol.68 , pp. 368-380
    • Smart, O.S.1
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 47
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Calpha geometry: Phi,psi and Cbeta deviation
    • Lovell, S. C. et al. Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins 50, 437-450 (2003).
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1
  • 48
    • 78651277458 scopus 로고    scopus 로고
    • A series of PDB related databases for everyday needs
    • Joosten, R. P. et al. A series of PDB related databases for everyday needs. Nucleic Acids Res. 39, D411-D419 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. D411-D419
    • Joosten, R.P.1
  • 49
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 50
    • 68549111266 scopus 로고    scopus 로고
    • PINE-SPARKY: Graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy
    • Lee, W., Westler, W. M., Bahrami, A., Eghbalnia, H. R. & Markley, J. L. PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy. Bioinformatics 25, 2085-2087 (2009).
    • (2009) Bioinformatics , vol.25 , pp. 2085-2087
    • Lee, W.1    Westler, W.M.2    Bahrami, A.3    Eghbalnia, H.R.4    Markley, J.L.5
  • 52
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirecttransform methods using perceptual criteria
    • Svergun, D. I. Determination of the regularization parameter in indirecttransform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503 (1992).
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 53
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 54
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V. & Svergun, D. I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864 (2003).
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 55
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.