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Volumn 3, Issue 10, 2012, Pages 1409-1413

Carbon-detected 15N NMR spin relaxation of an intrinsically disordered protein: FCP1 dynamics unbound and in complex with RAP74

Author keywords

[No Author keywords available]

Indexed keywords

3D STRUCTURE; BACKBONE DYNAMICS; DETECTION EXPERIMENTS; DIRECT CONTACT; DISORDERED PROTEINS; DYNAMIC ENSEMBLE; PARALLEL ANALYSIS; SPIN RELAXATION;

EID: 84862074830     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/jz300432e     Document Type: Article
Times cited : (28)

References (36)
  • 1
  • 2
    • 79958044914 scopus 로고    scopus 로고
    • Unstructural Biology Coming of Age
    • Tompa, P. Unstructural Biology Coming of Age Curr. Opin. Struct. Biol. 2011, 21, 419-425
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 419-425
    • Tompa, P.1
  • 3
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically Unstructured Proteins and Their Functions
    • Dyson, H. J.; Wright, P. E. Intrinsically Unstructured Proteins and Their Functions Nature Rev. Mol. Cell Biol. 2005, 6, 197-208
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 4
    • 81555225908 scopus 로고    scopus 로고
    • The Expanding View of Protein-Protein Interactions: Complexes Involving Intrinsically Disordered Proteins
    • Mészáros, B.; Simon, I.; Dosztányi, Z. The Expanding View of Protein-Protein Interactions: Complexes Involving Intrinsically Disordered Proteins Phys. Biol. 2011, 8, 035010
    • (2011) Phys. Biol. , vol.8 , pp. 035010
    • Mészáros, B.1    Simon, I.2    Dosztányi, Z.3
  • 5
    • 77957231785 scopus 로고    scopus 로고
    • Induced Fit, Conformational Selection and Independent Dynamic Segments: An Extended View of Binding Events
    • Csermely, P.; Palotai, R.; Nussinov, R. Induced Fit, Conformational Selection and Independent Dynamic Segments: An Extended View of Binding Events Trends Biochem. Sci. 2010, 35, 539-546
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 7
    • 77951631601 scopus 로고    scopus 로고
    • Structure/Function Implications in a Dynamic Complex of the Intrinsically Disordered Sic1 with the Cdc4 Subunit of an Scf Ubiquitin Ligase
    • Mittag, T.; Marsh, J.; Grishaev, A.; Orlicky, S.; Lin, H.; Sicheri, F.; Tyers, M.; Forman-Kay, J. D. Structure/Function Implications in a Dynamic Complex of the Intrinsically Disordered Sic1 with the Cdc4 Subunit of an Scf Ubiquitin Ligase Structure 2010, 18, 494-506
    • (2010) Structure , vol.18 , pp. 494-506
    • Mittag, T.1    Marsh, J.2    Grishaev, A.3    Orlicky, S.4    Lin, H.5    Sicheri, F.6    Tyers, M.7    Forman-Kay, J.D.8
  • 8
    • 79952489792 scopus 로고    scopus 로고
    • Topology-Based Modeling of Intrinsically Disordered Proteins: Balancing Intrinsic Folding and Intermolecular Interactions
    • Ganguly, D.; Chen, J. Topology-Based Modeling of Intrinsically Disordered Proteins: Balancing Intrinsic Folding and Intermolecular Interactions Proteins 2011, 79, 1251-1266
    • (2011) Proteins , vol.79 , pp. 1251-1266
    • Ganguly, D.1    Chen, J.2
  • 9
    • 73949144611 scopus 로고    scopus 로고
    • Toward a Quantitative Theory of Intrinsically Disordered Proteins and Their Function
    • Liu, J.; Faeder, J. R.; Camacho, C. J. Toward a Quantitative Theory of Intrinsically Disordered Proteins and Their Function Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 19819-19823
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 19819-19823
    • Liu, J.1    Faeder, J.R.2    Camacho, C.J.3
  • 12
    • 58049216739 scopus 로고    scopus 로고
    • Structural and Dynamic Characterization of Intrinsically Disordered Human Securin by NMR Spectroscopy
    • Csizmok, V.; Felli, I. C.; Tompa, P.; Banci, L.; Bertini, I. Structural and Dynamic Characterization of Intrinsically Disordered Human Securin by NMR Spectroscopy J. Am. Chem. Soc. 2008, 130, 16873-16879
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16873-16879
    • Csizmok, V.1    Felli, I.C.2    Tompa, P.3    Banci, L.4    Bertini, I.5
  • 13
    • 67349216108 scopus 로고    scopus 로고
    • H-Start for Exclusively Heteronuclear NMR Spectroscopy: The Case of Intrinsically Disordered Proteins
    • Bermel, W.; Bertini, I.; Csizmok, V.; Felli, I. C.; Pierattelli, R.; Tompa, P. H-Start for Exclusively Heteronuclear NMR Spectroscopy: The Case of Intrinsically Disordered Proteins J. Magn. Reson. 2009, 198, 275-281
    • (2009) J. Magn. Reson. , vol.198 , pp. 275-281
    • Bermel, W.1    Bertini, I.2    Csizmok, V.3    Felli, I.C.4    Pierattelli, R.5    Tompa, P.6
  • 14
    • 70449526424 scopus 로고    scopus 로고
    • Nmr Assignment of the Intrinsically Disordered C-Terminal Region of Homo Sapiens FCP1 in the Unbound State
    • Showalter, S. A. Nmr Assignment of the Intrinsically Disordered C-Terminal Region of Homo Sapiens FCP1 in the Unbound State Biomol. NMR Assign. 2009, 3, 179-181
    • (2009) Biomol. NMR Assign. , vol.3 , pp. 179-181
    • Showalter, S.A.1
  • 15
    • 69949152637 scopus 로고    scopus 로고
    • 13C-Direct Detected Spectroscopy of Intrinsically Disordered Proteins in Solution
    • 13C-Direct Detected Spectroscopy of Intrinsically Disordered Proteins in Solution J. Magn. Reson. 2009, 200, 354-358
    • (2009) J. Magn. Reson. , vol.200 , pp. 354-358
    • O'Hare, B.1    Benesi, A.J.2    Showalter, S.A.3
  • 16
    • 33645452144 scopus 로고    scopus 로고
    • Protonless NMR Experiments for Sequence-Specific Assignment of Backbone Nuclei in Unfolded Proteins
    • Bermel, W.; Bertini, I.; Felli, I. C.; Lee, Y. M.; Luchinat, C.; Pierattelli, R. Protonless NMR Experiments for Sequence-Specific Assignment of Backbone Nuclei in Unfolded Proteins J. Am. Chem. Soc. 2006, 128, 3918-3919
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3918-3919
    • Bermel, W.1    Bertini, I.2    Felli, I.C.3    Lee, Y.M.4    Luchinat, C.5    Pierattelli, R.6
  • 17
    • 47549107854 scopus 로고    scopus 로고
    • Direct 13C-Detection for Carbonyl Relaxation Studies of Protein Dynamics
    • Pasat, G.; Zintsmaster, J. S.; Peng, J. W. Direct 13C-Detection for Carbonyl Relaxation Studies of Protein Dynamics J. Magn. Reson. 2008, 193, 226-232
    • (2008) J. Magn. Reson. , vol.193 , pp. 226-232
    • Pasat, G.1    Zintsmaster, J.S.2    Peng, J.W.3
  • 18
    • 77049088258 scopus 로고    scopus 로고
    • Exclusively Heteronuclear NMR Experiments to Obtain Structural and Dynamic Information on Proteins
    • Bermel, W.; Bertini, I.; Felli, I. C.; Peruzzini, R.; Pierattelli, R. Exclusively Heteronuclear NMR Experiments to Obtain Structural and Dynamic Information on Proteins ChemPhysChem 2010, 11, 689-695
    • (2010) ChemPhysChem , vol.11 , pp. 689-695
    • Bermel, W.1    Bertini, I.2    Felli, I.C.3    Peruzzini, R.4    Pierattelli, R.5
  • 21
    • 0345701300 scopus 로고    scopus 로고
    • Molecular Mechanism of Recruitment of TFIIF-Associating RNA Polymerase C-Terminal Domain Phosphatase (FCP1) by Transcription Factor IIF
    • Kamada, K.; Roeder, R. G.; Burley, S. K. Molecular Mechanism of Recruitment of TFIIF-Associating RNA Polymerase C-Terminal Domain Phosphatase (FCP1) by Transcription Factor IIF Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 2296-2299
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 2296-2299
    • Kamada, K.1    Roeder, R.G.2    Burley, S.K.3
  • 22
    • 79960040425 scopus 로고    scopus 로고
    • The Disordered C-Terminus of the RNA Polymerase II Phosphatase FCP1 Is Partially Helical in the Unbound State
    • Lawrence, C. W.; Bonny, A.; Showalter, S. A. The Disordered C-Terminus of the RNA Polymerase II Phosphatase FCP1 Is Partially Helical in the Unbound State Biochem. Biophys. Res. Commun. 2011, 410, 461-465
    • (2011) Biochem. Biophys. Res. Commun. , vol.410 , pp. 461-465
    • Lawrence, C.W.1    Bonny, A.2    Showalter, S.A.3
  • 23
    • 81555228450 scopus 로고    scopus 로고
    • Atomistic Simulations Reveal Structural Disorder in the RAP74-FCP1 Complex
    • Wostenberg, C.; Kumar, S.; Noid, W. G.; Showalter, S. A. Atomistic Simulations Reveal Structural Disorder in the RAP74-FCP1 Complex J. Phys. Chem. B 2011, 115, 13731-13739
    • (2011) J. Phys. Chem. B , vol.115 , pp. 13731-13739
    • Wostenberg, C.1    Kumar, S.2    Noid, W.G.3    Showalter, S.A.4
  • 24
  • 25
    • 0347367040 scopus 로고    scopus 로고
    • Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCPI-Binding Sites of RAP74 and Human TFIIB
    • Nguyen, B. D.; Chen, H. T.; Kobor, M. S.; Greenblatt, J.; Legault, P.; Omichinski, J. G. Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCPI-Binding Sites of RAP74 and Human TFIIB Biochemistry 2003, 42, 1460-1469
    • (2003) Biochemistry , vol.42 , pp. 1460-1469
    • Nguyen, B.D.1    Chen, H.T.2    Kobor, M.S.3    Greenblatt, J.4    Legault, P.5    Omichinski, J.G.6
  • 27
    • 33646719091 scopus 로고
    • Model-Free Approach to the Interpretation of Nuclear Magnetic Resonance Relaxation in Macromolecules. 1. Theory and Range of Validity
    • Lipari, G.; Szabo, A. Model-Free Approach to the Interpretation of Nuclear Magnetic Resonance Relaxation in Macromolecules. 1. Theory and Range of Validity J. Am. Chem. Soc. 1982, 104, 4546-4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 28
    • 0028941877 scopus 로고
    • Backbone Dynamics of Escherichia Coli Ribonuclease HI: Correlations with Structure and Function in an Active Enzyme
    • Mandel, A. M.; Akke, M.; Palmer, A. G. Backbone Dynamics of Escherichia Coli Ribonuclease HI: Correlations with Structure and Function in an Active Enzyme J. Mol. Biol. 1995, 246, 144-163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 29
    • 0031111153 scopus 로고    scopus 로고
    • Rotational Diffusion Anisotropy of Proteins from Simultaneous Analysis of 15N and 13C Alpha Nuclear Spin Relaxation
    • Lee, L. K.; Rance, M.; Chazin, W. J.; Palmer, A. G. Rotational Diffusion Anisotropy of Proteins from Simultaneous Analysis of 15N and 13C Alpha Nuclear Spin Relaxation J. Biomol. NMR 1997, 9, 287-298
    • (1997) J. Biomol. NMR , vol.9 , pp. 287-298
    • Lee, L.K.1    Rance, M.2    Chazin, W.J.3    Palmer, A.G.4
  • 30
    • 0035853033 scopus 로고    scopus 로고
    • Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor IIF
    • Kamada, K.; De Angelis, J.; Roeder, R. G.; Burley, S. K. Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor IIF Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 3115-3120
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3115-3120
    • Kamada, K.1    De Angelis, J.2    Roeder, R.G.3    Burley, S.K.4
  • 32
    • 34548189188 scopus 로고    scopus 로고
    • Structural Characterization of the Intrinsically Unfolded Protein Beta-Synuclein, a Natural Negative Regulator of Alpha-Synuclein Aggregation
    • Bertoncini, C. W.; Rasia, R. M.; Lamberto, G. R.; Binolfi, A.; Zweckstetter, M.; Griesinger, C.; Fernandez, C. O. Structural Characterization of the Intrinsically Unfolded Protein Beta-Synuclein, a Natural Negative Regulator of Alpha-Synuclein Aggregation J. Mol. Biol. 2007, 372, 708-722
    • (2007) J. Mol. Biol. , vol.372 , pp. 708-722
    • Bertoncini, C.W.1    Rasia, R.M.2    Lamberto, G.R.3    Binolfi, A.4    Zweckstetter, M.5    Griesinger, C.6    Fernandez, C.O.7
  • 33
    • 45849117986 scopus 로고    scopus 로고
    • Backbone Dynamics of the 18.5 Kda Isoform of Myelin Basic Protein Reveals Transient Alpha-Helices and a Calmodulin-Binding Site
    • Libich, D. S.; Harauz, G. Backbone Dynamics of the 18.5 Kda Isoform of Myelin Basic Protein Reveals Transient Alpha-Helices and a Calmodulin-Binding Site Biophys. J. 2008, 94, 4847-4866
    • (2008) Biophys. J. , vol.94 , pp. 4847-4866
    • Libich, D.S.1    Harauz, G.2
  • 35
    • 64549121509 scopus 로고    scopus 로고
    • NMR Structure of a Complex Formed by the Carboxyl-Terminal Domain of Human RAP74 and a Phosphorylated Peptide from the Central Domain of the FCP1 Phosphatase
    • Yang, A.; Abbott, K. L.; Desjardins, A.; Di Lello, P.; Omichinski, J. G.; Legault, P. NMR Structure of a Complex Formed by the Carboxyl-Terminal Domain of Human RAP74 and a Phosphorylated Peptide from the Central Domain of the FCP1 Phosphatase Biochemistry 2009, 48, 1964-1974
    • (2009) Biochemistry , vol.48 , pp. 1964-1974
    • Yang, A.1    Abbott, K.L.2    Desjardins, A.3    Di Lello, P.4    Omichinski, J.G.5    Legault, P.6
  • 36
    • 80051927358 scopus 로고    scopus 로고
    • Incomplete Folding Upon Binding Mediates Cdk4/Cyclin D Complex Activation by Tyrosine Phosphorylation of Inhibitor p27 Protein
    • Ou, L.; Ferreira, A. M.; Otieno, S.; Xiao, L.; Bashford, D.; Kriwacki, R. W. Incomplete Folding Upon Binding Mediates Cdk4/Cyclin D Complex Activation by Tyrosine Phosphorylation of Inhibitor p27 Protein J. Biol. Chem. 2011, 286, 30142-30151
    • (2011) J. Biol. Chem. , vol.286 , pp. 30142-30151
    • Ou, L.1    Ferreira, A.M.2    Otieno, S.3    Xiao, L.4    Bashford, D.5    Kriwacki, R.W.6


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