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Volumn 324, Issue 4, 2002, Pages 587-597

Solvent exposed non-contacting amino acids play a critical role in NF-κB/IκBα complex formation

Author keywords

I B ; NF B; Protein protein interactions; Transcription factors; X ray crystallography

Indexed keywords

AMINO ACID; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; POLYPEPTIDE; PROTEIN; PROTEIN P50; PROTEIN P60; PROTEIN SUBUNIT; SERINE; SOLVENT; UNCLASSIFIED DRUG;

EID: 0036931719     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01149-X     Document Type: Article
Times cited : (30)

References (38)
  • 1
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin, A. S. (1996). The NF-κB and IκB proteins: New discoveries and insights. Annu. Rev. Immunol. 14, 649-683.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin, A.S.1
  • 2
    • 0031897632 scopus 로고    scopus 로고
    • NF-κB and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh, S., May, M. J. & Kopp, E. B. (1998). NF-κB and Rel proteins: Evolutionarily conserved mediators of immune responses. Annu. Rev. Immunol. 16, 225-260.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 3
    • 0033595892 scopus 로고    scopus 로고
    • The Rel/NF-κB signal transduction pathway: Introduction
    • Gilmore, T. D. (1999). The Rel/NF-κB signal transduction pathway: Introduction. Oncogene, 18, 6842-6844.
    • (1999) Oncogene , vol.18 , pp. 6842-6844
    • Gilmore, T.D.1
  • 4
    • 0035883151 scopus 로고    scopus 로고
    • NF-κB signaling pathways in mammalian and insect innate immunity
    • Silverman, N. & Maniatis, T. (2001). NF-κB signaling pathways in mammalian and insect innate immunity. Genes Dev. 15, 2321-2342.
    • (2001) Genes Dev. , vol.15 , pp. 2321-2342
    • Silverman, N.1    Maniatis, T.2
  • 6
    • 0031126395 scopus 로고    scopus 로고
    • IκB proteins: Structure, function and regulation
    • Whiteside, S. T. & Israël, A. (1997). IκB proteins: Structure, function and regulation. Semin. Cancer Biol. 8, 75-82.
    • (1997) Semin. Cancer Biol. , vol.8 , pp. 75-82
    • Whiteside, S.T.1    Israël, A.2
  • 7
    • 0026758170 scopus 로고
    • The candidate oncoprotein Bcl-3 is an antagonist of p50/NF-κB-mediated inhibition
    • Franzoso, G., Bours, V., Park, S., Tomita-Yamaguchi, M., Kelly, K. & Siebenlist, U. (1992). The candidate oncoprotein Bcl-3 is an antagonist of p50/NF-κB-mediated inhibition. Nature, 359, 339-342.
    • (1992) Nature , vol.359 , pp. 339-342
    • Franzoso, G.1    Bours, V.2    Park, S.3    Tomita-Yamaguchi, M.4    Kelly, K.5    Siebenlist, U.6
  • 8
    • 0027190466 scopus 로고
    • KBF1 (p50 NF-κB homodimer) acts as a repressor of H-2K-b gene expression in metastatic tumor cells
    • Plaksin, D., Baeuerle, P. A. & Eisenbach, L. (1993). KBF1 (p50 NF-κB homodimer) acts as a repressor of H-2K-b gene expression in metastatic tumor cells. J. Expt. Med. 177, 1651-1662.
    • (1993) J. Expt. Med. , vol.177 , pp. 1651-1662
    • Plaksin, D.1    Baeuerle, P.A.2    Eisenbach, L.3
  • 9
    • 0028986194 scopus 로고
    • IκBβ regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J. E., Phillips, R. J., Erdjument-Bromage, H., Tempst, P. & Ghosh, S. (1995). IκBβ regulates the persistent response in a biphasic activation of NF-κB. Cell, 80, 573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 10
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation
    • Huxford, T., Huang, D.-B., Malek, S. & Ghosh, G. (1998). The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell, 95, 759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.-B.2    Malek, S.3    Ghosh, G.4
  • 11
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs, M. D. & Harrison, S. C. (1998). Structure of an IκBα/NF-κB complex. Cell, 95, 749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 13
    • 0026783210 scopus 로고
    • IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg, A. A., Ruben, S. M., Scheinman, R. I., Haskill, S., Rosen, C. A. & Baldwin, A. S., Jr (1992). IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention. Genes Dev. 6, 1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin A.S., Jr.6
  • 15
    • 0028979479 scopus 로고
    • Structure of NF-κB p50 homodimer bound to a κB site
    • Ghosh, G., Van Duyne, G., Ghosh, S. & Sigler, P. B. (1995). Structure of NF-κB p50 homodimer bound to a κB site. Nature, 373, 303-310.
    • (1995) Nature , vol.373 , pp. 303-310
    • Ghosh, G.1    Van Duyne, G.2    Ghosh, S.3    Sigler, P.B.4
  • 17
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen, F. E., Huang, D.-B., Chen, Y.-Q. & Ghosh, G. (1998). Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature, 391, 410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.-B.2    Chen, Y.-Q.3    Ghosh, G.4
  • 19
    • 0035815111 scopus 로고    scopus 로고
    • Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB
    • Hughes, C. A., Mandell, J. G., Anand, G. S., Stock, A. M. & Komives, E. A. (2001). Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB. J. Mol. Biol. 307, 967-976.
    • (2001) J. Mol. Biol. , vol.307 , pp. 967-976
    • Hughes, C.A.1    Mandell, J.G.2    Anand, G.S.3    Stock, A.M.4    Komives, E.A.5
  • 20
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A. A. & Thorn, K. S. (1998). Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 21
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L., Chothia, C. & Janin, J. (1999). The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 22
    • 0030963761 scopus 로고    scopus 로고
    • Structure and dynamics of the glucocorticoid receptor DNA-binding domain: Comparison of wild-type and a mutant and altered specificity
    • Berglund, H., Wolf-Watz, M., Lundback, T., Van Den Berg, S. & Hard, T. (1997). Structure and dynamics of the glucocorticoid receptor DNA-binding domain: Comparison of wild-type and a mutant and altered specificity. Biochemistry, 36, 11188-11197.
    • (1997) Biochemistry , vol.36 , pp. 11188-11197
    • Berglund, H.1    Wolf-Watz, M.2    Lundback, T.3    Van den Berg, S.4    Hard, T.5
  • 23
    • 0036305609 scopus 로고    scopus 로고
    • Effects of the N2144S mutation on backbone dynamics of a TB-cbEGF domain pair from human fibrillin-1
    • Yuan, X., Werner, J. M., Lack, J., Knott, V., Handford, P. A., Campbell, I. D. & Downing, A. K. (2002). Effects of the N2144S mutation on backbone dynamics of a TB-cbEGF domain pair from human fibrillin-1. J. Mol. Biol. 316, 113-125.
    • (2002) J. Mol. Biol. , vol.316 , pp. 113-125
    • Yuan, X.1    Werner, J.M.2    Lack, J.3    Knott, V.4    Handford, P.A.5    Campbell, I.D.6    Downing, A.K.7
  • 24
    • 0034111186 scopus 로고    scopus 로고
    • Allosteric drugs: Thinking outside the active-site box
    • DeDecker, B. S. (2000). Allosteric drugs: Thinking outside the active-site box. Chem. Biol. 7, R103-R107.
    • (2000) Chem. Biol. , vol.7
    • DeDecker, B.S.1
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. Sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0032992292 scopus 로고    scopus 로고
    • Construction, expression, purification and functional analysis of recombinant NF-κB p50/p65 heterodimer
    • Chen, F. E., Kempiak, S., Huang, D.-B., Phelps, C. & Ghosh, G. (1999). Construction, expression, purification and functional analysis of recombinant NF-κB p50/p65 heterodimer. Protein Eng. 12, 423-428.
    • (1999) Protein Eng. , vol.12 , pp. 423-428
    • Chen, F.E.1    Kempiak, S.2    Huang, D.-B.3    Phelps, C.4    Ghosh, G.5
  • 27
    • 0034693271 scopus 로고    scopus 로고
    • Preparation and crystallization of dynamic NF-κB/IκB complexes
    • Huxford, T., Malek, S. & Ghosh, G. (2000). Preparation and crystallization of dynamic NF-κB/IκB complexes. J. Biol. Chem. 275, 32800-32806.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32800-32806
    • Huxford, T.1    Malek, S.2    Ghosh, G.3
  • 28
    • 0032566439 scopus 로고    scopus 로고
    • IκBα functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-κB
    • Malek, S., Huxford, T. & Ghosh, G. (1998). IκBα functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-κB. J. Biol. Chem. 273, 25427-25435.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25427-25435
    • Malek, S.1    Huxford, T.2    Ghosh, G.3
  • 29
    • 0035976962 scopus 로고    scopus 로고
    • IκBβ, but not IκBα, functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both nf-κb nuclear localization sequences in resting cells
    • Malek, S., Chen, Y., Huxford, T. & Ghosh, G. (2001). IκBβ, but not IκBα, functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both nf-κb nuclear localization sequences in resting cells. J. Biol. Chem. 276, 45225-45235.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45225-45235
    • Malek, S.1    Chen, Y.2    Huxford, T.3    Ghosh, G.4
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0031573470 scopus 로고    scopus 로고
    • The role of DNA in the mechanism of NF-κB dimer formation: Crystal structures of the dimerization domains of the p50 and p65 subunits
    • Huang, D.-B., Huxford, T., Chen, Y.-Q. & Ghosh, G. (1997). The role of DNA in the mechanism of NF-κB dimer formation: Crystal structures of the dimerization domains of the p50 and p65 subunits. Structure, 5, 1427-1436.
    • (1997) Structure , vol.5 , pp. 1427-1436
    • Huang, D.-B.1    Huxford, T.2    Chen, Y.-Q.3    Ghosh, G.4
  • 32
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography + NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse, K. R. W. et al. (1998). Crystallography + NMR system: A new software suite for macromolecular structure determination. Acta Crystallog. Sect. D, 54, 905-921.
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3    DeLano, W.L.4    Gros, P.5    Grosse, K.R.W.6
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0032428378 scopus 로고    scopus 로고
    • Identification of protein-protein interfaces by decreased amide proton solvent accessibility
    • Mandell, J. G., Falick, A. M. & Komives, E. A. (1998). Identification of protein-protein interfaces by decreased amide proton solvent accessibility. Proc. Natl Acad. Sci. USA, 95, 14705-14710.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14705-14710
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 35
    • 0032186122 scopus 로고    scopus 로고
    • Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
    • Mandell, J. G., Falick, A. M. & Komives, E. A. (1998). Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Anal. Chem. 70, 3987-3995.
    • (1998) Anal. Chem. , vol.70 , pp. 3987-3995
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 36
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 37
    • 0030815133 scopus 로고    scopus 로고
    • RASTER3D: Photorealistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. (1997). RASTER3D: Photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 38
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: Graphical representation and analysis of surface properties. Biophys. J. 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


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