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Volumn 23, Issue 4, 2014, Pages 464-480

The dynamics of interleukin-8 and its interaction with human CXC receptor i peptide

Author keywords

Dimer; Dynamics; Human CXC receptor 1; Interleukin 8; NMR

Indexed keywords

CHEMOKINE RECEPTOR CXCR1; INTERLEUKIN 8; PEPTIDE;

EID: 84900456625     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2430     Document Type: Article
Times cited : (26)

References (63)
  • 1
    • 58149232586 scopus 로고    scopus 로고
    • The interleukin-8 pathway in cancer
    • Waugh DJJ, Wilson C (2008) The interleukin-8 pathway in cancer. Clin Cancer Res 14:6735-6741
    • (2008) Clin Cancer Res , vol.14 , pp. 6735-6741
    • Waugh, D.J.J.1    Wilson, C.2
  • 2
    • 0035256994 scopus 로고    scopus 로고
    • Chemokines: Immunology?s high impact factors
    • Mackay CR (2001) Chemokines: Immunology?s high impact factors. Nat Immunol 2:95-101
    • (2001) Nat Immunol , vol.2 , pp. 95-101
    • Mackay, C.R.1
  • 3
    • 34247855761 scopus 로고    scopus 로고
    • Chemokine: Receptor structure, interactions, and antagonism
    • Allen SJ, Crown SE, Handel TM (2007) Chemokine: Receptor structure, interactions, and antagonism. Annu Rev Immunol 25:787-820
    • (2007) Annu Rev Immunol , vol.25 , pp. 787-820
    • Allen, S.J.1    Crown, S.E.2    Handel, T.M.3
  • 4
    • 0036178483 scopus 로고    scopus 로고
    • Structure, function, and inhibition of chemokines
    • Fernandez EJ, Lolis E (2002) Structure, function, and inhibition of chemokines. Annu Rev Pharmacol Toxicol 42:469-499
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 469-499
    • Fernandez, E.J.1    Lolis, E.2
  • 5
    • 33845599535 scopus 로고    scopus 로고
    • Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain
    • Fernando H, Nagle GT, Rajarathnam K (2007) Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain. FEBS J 274:241-251
    • (2007) FEBS J , vol.274 , pp. 241-251
    • Fernando, H.1    Nagle, G.T.2    Rajarathnam, K.3
  • 6
    • 0028971068 scopus 로고
    • H-1- NMR solution structure of an active monomeric interleukin- 8
    • Rajarathnam K, Clarklewis I, Sykes BD (1995) H-1- NMR solution structure of an active monomeric interleukin- 8. Biochemistry 34:12983-12990
    • (1995) Biochemistry , vol.34 , pp. 12983-12990
    • Rajarathnam, K.1    Clarklewis, I.2    Sykes, B.D.3
  • 7
    • 70349146698 scopus 로고    scopus 로고
    • Structural basis for differential binding of the interleukin-8 monomer and dimer to the CXCR1 N-domain: Role of coupled interactions and dynamics
    • Ravindran A, Joseph PR, Rajarathnam K (2009) Structural basis for differential binding of the interleukin-8 monomer and dimer to the CXCR1 N-domain: Role of coupled interactions and dynamics. Biochemistry 48: 8795-8805
    • (2009) Biochemistry , vol.48 , pp. 8795-8805
    • Ravindran, A.1    Joseph, P.R.2    Rajarathnam, K.3
  • 8
    • 0028800935 scopus 로고
    • High activity suppression of myeloid progenitor proliferation by chimeric mutants of interleukin 8 and platelet factor 4
    • Daly TJ, LaRosa GJ, Dolich S, Maione TE, Cooper S, Broxmeyer HE (1995) High activity suppression of myeloid progenitor proliferation by chimeric mutants of interleukin 8 and platelet factor 4. J Biol Chem 270: 23282-23292
    • (1995) J Biol Chem , vol.270 , pp. 23282-23292
    • Daly, T.J.1    Larosa, G.J.2    Dolich, S.3    Maione, T.E.4    Cooper, S.5    Broxmeyer, H.E.6
  • 9
    • 0033081379 scopus 로고    scopus 로고
    • Structure of a CXC chemokine-receptor fragment in complex with interleukin-8
    • Skelton NJ, Quan C, Reilly D, Lowman H (1999) Structure of a CXC chemokine-receptor fragment in complex with interleukin-8. Structure 7:157-168
    • (1999) Structure , vol.7 , pp. 157-168
    • Skelton, N.J.1    Quan, C.2    Reilly, D.3    Lowman, H.4
  • 12
    • 0026333179 scopus 로고
    • Structure-activity relationships of interleukin-8 determined using chemically synthesized analogs critical role of NH2-terminal residues and evidence for uncoupling of neutrophil chemotaxis, exocytosis, and receptor binding activities
    • Clark-Lewis I, Schumacher C, Baggiolini M, Moser B( 1991) Structure-activity relationships of interleukin-8 determined using chemically synthesized analogs. Critical role of NH2-terminal residues and evidence for uncoupling of neutrophil chemotaxis, exocytosis, and receptor binding activities. J Biol Chem 266:23128-23134
    • (1991) J Biol Chem , vol.266 , pp. 23128-23134
    • Clark-Lewis, I.1    Schumacher, C.2    Baggiolini, M.3    Moser, B.4
  • 14
    • 0026095795 scopus 로고
    • Structure and functional expression of a human interleukin-8 receptor
    • Holmes WE, Lee J, Kuang WJ, Rice GC, Wood WI( 1991) Structure and functional expression of a human interleukin-8 receptor. Science 253:1278-1280
    • (1991) Science , vol.253 , pp. 1278-1280
    • Holmes, W.E.1    Lee, J.2    Kuang, W.J.3    Rice, G.C.4    Wood, W.I.5
  • 15
    • 4344589888 scopus 로고    scopus 로고
    • Dimer dissociation is essential for interleukin-8 (IL-8) binding to CXCR1 receptor
    • Fernando H, Chin C, Rosgen J, Rajarathnam K (2004) Dimer dissociation is essential for interleukin-8 (IL-8) binding to CXCR1 receptor. J Biol Chem 279:36175-36178
    • (2004) J Biol Chem , vol.279 , pp. 36175-36178
    • Fernando, H.1    Chin, C.2    Rosgen, J.3    Rajarathnam, K.4
  • 16
  • 17
    • 81355146334 scopus 로고    scopus 로고
    • Interactions of interleukin-8 with the human chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy
    • Park SH, Casagrande F, Cho L, Albrecht L, Opella SJ( 2011) Interactions of interleukin-8 with the human chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy. J Mol Biol 414:194-203
    • (2011) J Mol Biol , vol.414 , pp. 194-203
    • Park, S.H.1    Casagrande, F.2    Cho, L.3    Albrecht, L.4    Opella, S.J.5
  • 19
    • 0028053158 scopus 로고
    • Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type-1 human interleukin-8 receptor
    • Clubb RT, Omichinski JG, Clore GM, Gronenborn AM( 1994) Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type-1 human interleukin-8 receptor. FEBS Lett 338:93-97
    • (1994) FEBS Lett , vol.338 , pp. 93-97
    • Clubb, R.T.1    Omichinski, J.G.2    Clore, G.M.3    Gronenborn, A.M.4
  • 20
    • 3142779910 scopus 로고    scopus 로고
    • Ligand selectivity and affinity of chemokine receptor CXCR1. Role of N-terminal domain
    • Rajagopalan L, Rajarathnam K (2004) Ligand selectivity and affinity of chemokine receptor CXCR1. Role of N-terminal domain. J Biol Chem 279:30000-30008
    • (2004) J Biol Chem , vol.279 , pp. 30000-30008
    • Rajagopalan, L.1    Rajarathnam, K.2
  • 21
    • 0027933626 scopus 로고
    • Complete mutagenesis of the extracellular domain of interleukin- 8 (IL-8) type A receptor identifies charged residues mediating IL-8 binding and signal transduction
    • Leong SR, Kabakoff RC, Hebert CA (1994) Complete mutagenesis of the extracellular domain of interleukin- 8 (IL-8) type A receptor identifies charged residues mediating IL-8 binding and signal transduction. J Biol Chem 269:19343-19348
    • (1994) J Biol Chem , vol.269 , pp. 19343-19348
    • Leong, S.R.1    Kabakoff, R.C.2    Hebert, C.A.3
  • 23
    • 0028212497 scopus 로고
    • Class II restricted T cell responses in theiler's murine encephalomyelitis virus-induced demyelinating disease. V. Mapping of a dominant immunopathologic VP2 T cell epitope in susceptible SJL/J mice
    • Gerety SJ, Karpus WJ, Cubbon AR, Goswami RG, Rundell MK, Peterson JD, Miller SD (1994) Class IIrestricted T cell responses in Theiler?s murine encephalomyelitis virus-induced demyelinating disease. V. Mapping of a dominant immunopathologic VP2 T cell epitope in susceptible SJL/J mice. J Immunol 152:908-918
    • (1994) J Immunol , vol.152 , pp. 908-918
    • Gerety, S.J.1    Karpus, W.J.2    Cubbon, A.R.3    Goswami, R.G.4    Rundell, M.K.5    Peterson, J.D.6    Miller, S.D.7
  • 24
    • 0142149116 scopus 로고    scopus 로고
    • Detection of nano-second internal motion and determination of overall tumbling times independent of the time scale of internal motion in proteins from NMR relaxation data
    • Larsson G, Martinez G, Schleucher J, Wijmenga SS( 2003) Detection of nano-second internal motion and determination of overall tumbling times independent of the time scale of internal motion in proteins from NMR relaxation data. J Biomol NMR 27:291-312
    • (2003) J Biomol NMR , vol.27 , pp. 291-312
    • Larsson, G.1    Martinez, G.2    Schleucher, J.3    Wijmenga, S.S.4
  • 25
    • 28844480494 scopus 로고    scopus 로고
    • Effective rotational correlation times of proteins from NMR relaxation interference
    • Lee D, Hilty C, Wider G, Wuthrich K (2006) Effective rotational correlation times of proteins from NMR relaxation interference. J Magn Reson 178:72-76
    • (2006) J Magn Reson , vol.178 , pp. 72-76
    • Lee, D.1    Hilty, C.2    Wider, G.3    Wuthrich, K.4
  • 27
    • 77952401424 scopus 로고    scopus 로고
    • NMR relaxation studies of an RNA-binding segment of the rous sarcoma virus gag polyprotein in free and bound states: A model for autoinhibition of assembly
    • Taylor GM, Ma L, Vogt VM, Post CB (2010) NMR relaxation studies of an RNA-binding segment of the rous sarcoma virus gag polyprotein in free and bound states: A model for autoinhibition of assembly. Biochemistry 49:4006-4017
    • (2010) Biochemistry , vol.49 , pp. 4006-4017
    • Taylor, G.M.1    Ma, L.2    Vogt, V.M.3    Post, C.B.4
  • 28
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • Kay LE, Torchia DA, Bax A (1989) Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease. Biochemistry 28:8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 29
    • 0033071795 scopus 로고    scopus 로고
    • Quantitative measurement of transverse and longitudinal cross-correlation between 13C-1H dipolar interaction and 13C chemical shift anisotropy: Application to a 13C-labeled DNA duplex
    • Kojima C, Ono A, Kainosho M, James TL (1999) Quantitative measurement of transverse and longitudinal cross-correlation between 13C-1H dipolar interaction and 13C chemical shift anisotropy: Application to a 13C-labeled DNA duplex. J Magn Reson 136:169-175
    • (1999) J Magn Reson , vol.136 , pp. 169-175
    • Kojima, C.1    Ono, A.2    Kainosho, M.3    James, T.L.4
  • 31
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K, Kern D (2007) Dynamic personalities of proteins. Nature 450:964-972
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 32
    • 33748619206 scopus 로고    scopus 로고
    • An NMR perspective on enzyme dynamics
    • Boehr DD, Dyson HJ, Wright PE (2006) An NMR perspective on enzyme dynamics. Chem Rev 106:3055-3079
    • (2006) Chem Rev , vol.106 , pp. 3055-3079
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 33
    • 0037120879 scopus 로고    scopus 로고
    • Reconstructing NMR spectra of invisible excited protein states using HSQC and HMQC experiments
    • Skrynnikov NR, Dahlquist FW, Kay LE (2002) Reconstructing NMR spectra of invisible excited protein states using HSQC and HMQC experiments. J Am Chem Soc 124:12352-12360
    • (2002) J Am Chem Soc , vol.124 , pp. 12352-12360
    • Skrynnikov, N.R.1    Dahlquist, F.W.2    Kay, L.E.3
  • 35
    • 0035819455 scopus 로고    scopus 로고
    • Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
    • Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE (2001) Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J Am Chem Soc 123:967-975
    • (2001) J Am Chem Soc , vol.123 , pp. 967-975
    • Mulder, F.A.1    Skrynnikov, N.R.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 36
    • 0030891853 scopus 로고    scopus 로고
    • Monomeric variants of IL-8: Effects of side chain substitutions and solution conditions upon dimer formation
    • Lowman HB, Fairbrother WJ, Slagle PH, Kabakoff R, Liu J, Shire S, Hebert CA (1997) Monomeric variants of IL-8: Effects of side chain substitutions and solution conditions upon dimer formation. Protein Sci 6:598-608
    • (1997) Protein Sci , vol.6 , pp. 598-608
    • Lowman, H.B.1    Fairbrother, W.J.2    Slagle, P.H.3    Kabakoff, R.4    Liu, J.5    Shire, S.6    Hebert, C.A.7
  • 37
    • 27544456339 scopus 로고    scopus 로고
    • A simple method to predict protein flexibility using secondary chemical shifts
    • Berjanskii MV, Wishart DS (2005) A simple method to predict protein flexibility using secondary chemical shifts. J Am Chem Soc 127:14970-14971
    • (2005) J Am Chem Soc , vol.127 , pp. 14970-14971
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 40
    • 84856728860 scopus 로고    scopus 로고
    • Microsecond time-scale conformational exchange in proteins: Using long molecular dynamics trajectory to simulate NMR relaxation dispersion data
    • Xue Y, Ward JM, Yuwen T, Podkorytov IS, Skrynnikov NR (2012) Microsecond time-scale conformational exchange in proteins: Using long molecular dynamics trajectory to simulate NMR relaxation dispersion data. J Am Chem Soc 134:2555-2562
    • (2012) J Am Chem Soc , vol.134 , pp. 2555-2562
    • Xue, Y.1    Ward, J.M.2    Yuwen, T.3    Podkorytov, I.S.4    Skrynnikov, N.R.5
  • 41
    • 84857845204 scopus 로고    scopus 로고
    • Characterization of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts
    • Camilloni C, Robustelli P, De Simone A, Cavalli A, Vendruscolo M (2012) Characterization of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts. J Am Chem Soc 134:3968-3971
    • (2012) J Am Chem Soc , vol.134 , pp. 3968-3971
    • Camilloni, C.1    Robustelli, P.2    De Simone, A.3    Cavalli, A.4    Vendruscolo, M.5
  • 42
    • 84858634014 scopus 로고    scopus 로고
    • Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts
    • Camilloni C, De Simone A, Vranken WF, Vendruscolo M (2012) Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts. Biochemistry 51: 2224-2231
    • (2012) Biochemistry , vol.51 , pp. 2224-2231
    • Camilloni, C.1    De Simone, A.2    Vranken, W.F.3    Vendruscolo, M.4
  • 43
    • 16244373398 scopus 로고    scopus 로고
    • Interleukin 8 dimerization as a mechanism for regulation of neutrophil adherence-dependent oxidant production
    • Williams MA, Cave CM, Quaid G, Robinson C, Daly TJ, Witt D, Lentsch AB, Solomkin JS (2005) Interleukin 8 dimerization as a mechanism for regulation of neutrophil adherence-dependent oxidant production. Shock 23:371-376
    • (2005) Shock , vol.23 , pp. 371-376
    • Williams, M.A.1    Cave, C.M.2    Quaid, G.3    Robinson, C.4    Daly, T.J.5    Witt, D.6    Lentsch, A.B.7    Solomkin, J.S.8
  • 44
    • 0031913371 scopus 로고    scopus 로고
    • IL-8 derivatives with a reduced potential to form homodimers are fully active in vitro and in vivo
    • Horcher M, Rot A, Aschauer H, Besemer J (1998) IL-8 derivatives with a reduced potential to form homodimers are fully active in vitro and in vivo. Cytokine 10:1-12
    • (1998) Cytokine , vol.10 , pp. 1-12
    • Horcher, M.1    Rot, A.2    Aschauer, H.3    Besemer, J.4
  • 45
    • 0035072684 scopus 로고    scopus 로고
    • Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex
    • Osborne MJ, Wright PE (2001) Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex. J Biomol NMR 19:209-230
    • (2001) J Biomol NMR , vol.19 , pp. 209-230
    • Osborne, M.J.1    Wright, P.E.2
  • 46
    • 0037076522 scopus 로고    scopus 로고
    • Evidence for flexibility in the function of ribonuclease A
    • Cole R, Loria JP (2002) Evidence for flexibility in the function of ribonuclease A. Biochemistry 41:6072-6081
    • (2002) Biochemistry , vol.41 , pp. 6072-6081
    • Cole, R.1    Loria, J.P.2
  • 47
    • 79953211861 scopus 로고    scopus 로고
    • Murine interleukin-3: Structure, dynamics, and conformational heterogeneity in solution
    • Yao S, Young IG, Norton RS, Murphy JM (2011) Murine interleukin-3: Structure, dynamics, and conformational heterogeneity in solution. Biochemistry 50:2464-2477
    • (2011) Biochemistry , vol.50 , pp. 2464-2477
    • Yao, S.1    Young, I.G.2    Norton, R.S.3    Murphy, J.M.4
  • 48
    • 0028362141 scopus 로고
    • Monomerdimer equilibria of interleukin-8 and neutrophilactivating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B
    • Schnitzel W, Monschein U, Besemer J (1994) Monomerdimer equilibria of interleukin-8 and neutrophilactivating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B. J Leuk Biol 55:763-770
    • (1994) J Leuk Biol , vol.55 , pp. 763-770
    • Schnitzel, W.1    Monschein, U.2    Besemer, J.3
  • 53
    • 0032719427 scopus 로고    scopus 로고
    • A TROSY CPMG sequence for characterizing chemical exchange in large proteins
    • Loria JP, Rance M, Palmer AG 3rd (1999) A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J Biomol NMR 15:151-155
    • (1999) J Biomol NMR , vol.15 , pp. 151-155
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 54
    • 84873905399 scopus 로고    scopus 로고
    • Assessment of the use of NMR chemical shifts as replicaaveraged structural restraints in molecular dynamics simulations to characterize the dynamics of proteins
    • Camilloni C, Cavalli A, Vendruscolo M (2013) Assessment of the use of NMR chemical shifts as replicaaveraged structural restraints in molecular dynamics simulations to characterize the dynamics of proteins. J Phys Chem B 117:1838-1843
    • (2013) J Phys Chem B , vol.117 , pp. 1838-1843
    • Camilloni, C.1    Cavalli, A.2    Vendruscolo, M.3
  • 55
    • 84874846601 scopus 로고    scopus 로고
    • Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle
    • Cavalli A, Camilloni C, Vendruscolo M (2013) Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle. J Chem Phys 138:094112
    • (2013) J Chem Phys , vol.138 , pp. 094112
    • Cavalli, A.1    Camilloni, C.2    Vendruscolo, M.3
  • 58
    • 17844386576 scopus 로고    scopus 로고
    • Comparison of sequence-based and structure-based energy functions for the reversible folding of a peptide
    • Cavalli A, Vendruscolo M, Paci E (2005) Comparison of sequence-based and structure-based energy functions for the reversible folding of a peptide. Biophys J 88: 3158-3166
    • (2005) Biophys J , vol.88 , pp. 3158-3166
    • Cavalli, A.1    Vendruscolo, M.2    Paci, E.3
  • 59
    • 79959720287 scopus 로고    scopus 로고
    • How robust are protein folding simulations with respect to force field parameterization?
    • Piana S, Lindorff-Larsen K, Shaw DE (2011) How robust are protein folding simulations with respect to force field parameterization? Biophys J 100:L47-49
    • (2011) Biophys J , vol.100
    • Piana, S.1    Lindorff-Larsen, K.2    Shaw, D.E.3
  • 60
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • Hess B (2008) P-LINCS: A parallel linear constraint solver for molecular simulation. J Chem Theory Comput 4:116-122
    • (2008) J Chem Theory Comput , vol.4 , pp. 116-122
    • Hess, B.1
  • 62
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi G, Donadio D, Parrinello M (2007) Canonical sampling through velocity rescaling. J Chem Phys 126: 014101
    • (2007) J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 63
    • 33947304702 scopus 로고    scopus 로고
    • PyMOL: A communications tool for computational models
    • DeLano WL, Lam JW (2005) PyMOL: A communications tool for computational models. Abstr Pap Am Chem Soc 230: U1371-U1372
    • (2005) Abstr Pap Am Chem Soc , vol.230
    • Delano, W.L.1    Lam, J.W.2


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