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Volumn 380, Issue 5, 2008, Pages 917-931

Transfer of Flexibility between Ankyrin Repeats in IκBα upon Formation of the NF-κB Complex

Author keywords

hydrogen exchange; NMR relaxation dynamics; TROSY

Indexed keywords

ANKYRIN; ANKYRIN 5; ANKYRIN 6; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN P50;

EID: 45849140515     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.05.048     Document Type: Article
Times cited : (57)

References (54)
  • 1
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: ten years after
    • Baeuerle P.A., and Baltimore D. NF-κB: ten years after. Cell 87 (1996) 13-20
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 2
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl H.L. Activators and target genes of Rel/NF-κB transcription factors. Oncogene 18 (1999) 6853-6866
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 3
    • 33750448661 scopus 로고    scopus 로고
    • Transcriptional regulation via the NF-κB signaling module
    • Hoffmann A., Natoli G., and Ghosh G. Transcriptional regulation via the NF-κB signaling module. Oncogene 25 (2006) 6706-6716
    • (2006) Oncogene , vol.25 , pp. 6706-6716
    • Hoffmann, A.1    Natoli, G.2    Ghosh, G.3
  • 4
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-κB: players, pathways, perspectives
    • Gilmore T.D. Introduction to NF-κB: players, pathways, perspectives. Oncogene 25 (2006) 6680-6684
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 5
    • 0022930702 scopus 로고
    • Inducibility of κ immunoglobulin enhancer-binding protein NF-κB by a posttranslational mechanism
    • Sen R., and Baltimore D. Inducibility of κ immunoglobulin enhancer-binding protein NF-κB by a posttranslational mechanism. Cell 47 (1986) 921-928
    • (1986) Cell , vol.47 , pp. 921-928
    • Sen, R.1    Baltimore, D.2
  • 6
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and I-κB proteins: new discoveries and insights
    • Baldwin A.S. The NF-κB and I-κB proteins: new discoveries and insights. Annu. Rev. Immunol. 14 (1996) 649-683
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin, A.S.1
  • 7
    • 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., and Ghosh G. IκBα functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-κB. J. Biol. Chem. 273 (1998) 25427-25435
    • (1998) J. Biol. Chem. , vol.273 , pp. 25427-25435
    • Malek, S.1    Huxford, T.2    Ghosh, G.3
  • 8
    • 0032217267 scopus 로고    scopus 로고
    • IκB-NF-κB structures: at the interface of inflammation control
    • Baeuerle P.A. IκB-NF-κB structures: at the interface of inflammation control. Cell 95 (1998) 729-731
    • (1998) Cell , vol.95 , pp. 729-731
    • Baeuerle, P.A.1
  • 9
    • 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., and Ghosh G. The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell 95 (1998) 759-770
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 10
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs M.D., and Harrison S.C. Structure of an IκBα/NF-κB complex. Cell 95 (1998) 749-758
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 11
    • 0037482136 scopus 로고    scopus 로고
    • X-ray crystal structure of an IκBβ × NF-κB p65 homodimer complex
    • Malek S., Huang D.B., Huxford T., Ghosh S., and Ghosh G. X-ray crystal structure of an IκBβ × NF-κB p65 homodimer complex. J. Biol. Chem. 278 (2003) 23094-23100
    • (2003) J. Biol. Chem. , vol.278 , pp. 23094-23100
    • Malek, S.1    Huang, D.B.2    Huxford, T.3    Ghosh, S.4    Ghosh, G.5
  • 12
    • 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., and Ghosh G. 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 (2001) 45225-45235
    • (2001) J. Biol. Chem. , vol.276 , pp. 45225-45235
    • Malek, S.1    Chen, Y.2    Huxford, T.3    Ghosh, G.4
  • 13
    • 0033953587 scopus 로고    scopus 로고
    • A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes
    • Huang T.T., Kudo N., Yoshida M., and Miyamoto S. A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes. Proc. Natl Acad. Sci. USA 97 (2000) 1014-1019
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1014-1019
    • Huang, T.T.1    Kudo, N.2    Yoshida, M.3    Miyamoto, S.4
  • 14
    • 0344549859 scopus 로고    scopus 로고
    • Regulation of RelA subcellular localization by a putative nuclear export signal and p50
    • Harhaj E.W., and Sun S.C. Regulation of RelA subcellular localization by a putative nuclear export signal and p50. Mol. Cell Biol. 19 (1999) 7088-7095
    • (1999) Mol. Cell Biol. , vol.19 , pp. 7088-7095
    • Harhaj, E.W.1    Sun, S.C.2
  • 15
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden M.S., and Ghosh S. Signaling to NF-κB. Genes Dev. 18 (2004) 2195-2224
    • (2004) Genes Dev. , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 16
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi L.K., Cammett T.J., Desrosiers D.C., and Peng Z.Y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 13 (2004) 1435-1448
    • (2004) Protein Sci. , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4
  • 17
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M., and Rogers S.W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21 (1996) 267-271
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 18
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis
    • Rogers S., Wells R., and Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234 (1986) 364-368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 19
    • 3042628330 scopus 로고    scopus 로고
    • Biophysical characterization of the free IκBα ankyrin repeat domain in solution
    • Croy C.H., Bergqvist S., Huxford T., Ghosh G., and Komives E.A. Biophysical characterization of the free IκBα ankyrin repeat domain in solution. Protein Sci. 13 (2004) 1767-1777
    • (2004) Protein Sci. , vol.13 , pp. 1767-1777
    • Croy, C.H.1    Bergqvist, S.2    Huxford, T.3    Ghosh, G.4    Komives, E.A.5
  • 20
    • 33745276259 scopus 로고    scopus 로고
    • Thermodynamics reveal that helix four in the NLS of NF-κB p65 anchors IκBα, forming a very stable complex
    • Bergqvist S., Croy C.H., Kjaergaard M., Huxford T., Ghosh G., and Komives E.A. Thermodynamics reveal that helix four in the NLS of NF-κB p65 anchors IκBα, forming a very stable complex. J. Mol. Biol. 360 (2006) 421-434
    • (2006) J. Mol. Biol. , vol.360 , pp. 421-434
    • Bergqvist, S.1    Croy, C.H.2    Kjaergaard, M.3    Huxford, T.4    Ghosh, G.5    Komives, E.A.6
  • 21
    • 34447628760 scopus 로고    scopus 로고
    • Regions of IκBα that are critical for its inhibition of NF-κB·DNA interaction fold upon binding to NF-κB
    • Truhlar S.M., Torpey J.W., and Komives E.A. Regions of IκBα that are critical for its inhibition of NF-κB·DNA interaction fold upon binding to NF-κB. Proc. Natl. Acad. Sci. USA 103 (2006) 18951-18956
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18951-18956
    • Truhlar, S.M.1    Torpey, J.W.2    Komives, E.A.3
  • 22
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 25
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6 (2005) 197-208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 27
    • 43249110701 scopus 로고    scopus 로고
    • NF-κB dictates IκB degradation modes
    • Mathes E., O'Dea E., Hoffmann A., and Ghosh G. NF-κB dictates IκB degradation modes. EMBO J. 27 (2008) 1357-1367
    • (2008) EMBO J. , vol.27 , pp. 1357-1367
    • Mathes, E.1    O'Dea, E.2    Hoffmann, A.3    Ghosh, G.4
  • 28
  • 29
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers R., and Kay L.E. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445 (2007) 618-622
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 30
    • 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., and Ghosh G. Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391 (1998) 410-413
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 32
    • 0033518575 scopus 로고    scopus 로고
    • TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
    • Salzmann M., Wider G., Pervushin K., Senn H., and Wüthrich K. TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins. J. Am. Chem. Soc. 121 (1999) 844-848
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 844-848
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Senn, H.4    Wüthrich, K.5
  • 35
    • 0031027910 scopus 로고    scopus 로고
    • Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR
    • Gardner K.H., Rosen M.K., and Kay L.E. Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry 36 (1997) 1389-1401
    • (1997) Biochemistry , vol.36 , pp. 1389-1401
    • Gardner, K.H.1    Rosen, M.K.2    Kay, L.E.3
  • 36
    • 45849086996 scopus 로고
    • Internal motions in proteins and nucleic acids and their hydrogen exchange properties
    • [Comments]
    • Englander S.W. Internal motions in proteins and nucleic acids and their hydrogen exchange properties. [Comments]. Mol. Cell Biophys. 1 (1980) 15-28
    • (1980) Mol. Cell Biophys. , vol.1 , pp. 15-28
    • Englander, S.W.1
  • 37
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y., Milne J.S., Mayne L., and Englander S.W. Primary structure effects on peptide group hydrogen exchange. Proteins 17 (1993) 75-86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 40
    • 0001917325 scopus 로고
    • Deuterium exchange between peptides and water
    • Linderström-Lang K. Deuterium exchange between peptides and water. Chem. Soc. Spec. Publ. 2 (1955) 1-20
    • (1955) Chem. Soc. Spec. Publ. , vol.2 , pp. 1-20
    • Linderström-Lang, K.1
  • 41
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer D., and Wright P.E. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263 (1996) 531-538
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 42
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser V.J., and Thompson E.B. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc. Natl Acad. Sci. USA 104 (2007) 8311-8315
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 43
    • 44649146416 scopus 로고    scopus 로고
    • Truhlar, S. M., Mathes, E., Cervantes, C. F., Ghosh, G. & Komives, E. A. (2008). Pre-folding IκBα alters control of NF-κB signaling. J. Mol. Biol. In press. doi:10.1016/j.jmb.2008.02.053.
    • Truhlar, S. M., Mathes, E., Cervantes, C. F., Ghosh, G. & Komives, E. A. (2008). Pre-folding IκBα alters control of NF-κB signaling. J. Mol. Biol. In press. doi:10.1016/j.jmb.2008.02.053.
  • 45
    • 0036931719 scopus 로고    scopus 로고
    • Solvent exposed non-contacting amino acids play a critical role in NF-κB/IκBkα complex formation
    • Huxford T., Mishler D., Phelps C.B., Huang D.B., Sengchanthalangsy L.L., Reeves R., et al. Solvent exposed non-contacting amino acids play a critical role in NF-κB/IκBkα complex formation. J. Mol. Biol. 324 (2002) 587-597
    • (2002) J. Mol. Biol. , vol.324 , pp. 587-597
    • Huxford, T.1    Mishler, D.2    Phelps, C.B.3    Huang, D.B.4    Sengchanthalangsy, L.L.5    Reeves, R.6
  • 46
    • 0032992292 scopus 로고    scopus 로고
    • Construction, expression, purification and functional analysis of recombinant NFκB p50/p65 heterodimer
    • Chen F.E., Kempiak S., Huang D.B., Phelps C., and Ghosh G. Construction, expression, purification and functional analysis of recombinant NFκB p50/p65 heterodimer. Protein Eng. 12 (1999) 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
  • 47
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • Grzesiek S., and Bax A. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96 (1992) 432-440
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 48
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind M., and Mueller L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson. 101 (1993) 201-205
    • (1993) J. Magn. Reson. , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 51
    • 34249765651 scopus 로고
    • NMRView: a computer program for the visualization and analysis of NMR data
    • Johnson B.A., and Blevins R.A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4 (1994) 604-613
    • (1994) J. Biomol. NMR , vol.4 , pp. 604-613
    • Johnson, B.A.1    Blevins, R.A.2
  • 52
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., and Palmer A.G. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246 (1995) 144-163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 53
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115 (1993) 12593-12594
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 54
    • 0034183497 scopus 로고    scopus 로고
    • Clean TROSY: compensation for relaxation-induced artifacts
    • Schulte-Herbruggen T., and Sørensen O.W. Clean TROSY: compensation for relaxation-induced artifacts. J. Magn. Reson. 144 (2000) 123-128
    • (2000) J. Magn. Reson. , vol.144 , pp. 123-128
    • Schulte-Herbruggen, T.1    Sørensen, O.W.2


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