메뉴 건너뛰기




Volumn 456, Issue 2, 2013, Pages 241-251

Dynamic conformational switching in the chemokine ligand is essential for G-protein-coupled receptor activation

Author keywords

Chemokine; Conformational ensemble; G proteincoupled receptor; Long range coupling; Signalling

Indexed keywords

CHEMOKINE; G PROTEIN COUPLED RECEPTOR; GLYCINE; INTERLEUKIN 8; MITOGEN ACTIVATED PROTEIN KINASE; PROLINE; RADIOLIGAND;

EID: 84887415994     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130148     Document Type: Article
Times cited : (25)

References (62)
  • 2
    • 33750929921 scopus 로고    scopus 로고
    • Structural basis of chemokine receptor function: A model for binding affinity and ligand selectivity
    • Rajagopalan, L. and Rajarathnam, K. (2006) Structural basis of chemokine receptor function: a model for binding affinity and ligand selectivity. Biosci. Rep. 26, 325-339
    • (2006) Biosci. Rep , vol.26 , pp. 325-339
    • Rajagopalan, L.1    Rajarathnam, K.2
  • 4
    • 0242335085 scopus 로고    scopus 로고
    • Molecular characterization of the chemokine receptor CXCR3: Evidence for the involvement of distinct extracellular domains in a multi-step model of ligand binding and receptor activation
    • Xanthou, G., Williams, T. J. and Pease, J. E. (2003) Molecular characterization of the chemokine receptor CXCR3: evidence for the involvement of distinct extracellular domains in a multi-step model of ligand binding and receptor activation. Eur. J. Immunol. 33, 2927-2936
    • (2003) Eur. J. Immunol , vol.33 , pp. 2927-2936
    • Xanthou, G.1    Williams, T.J.2    Pease, J.E.3
  • 7
    • 0028305217 scopus 로고
    • Structural requirements for interleukin-8 function identified by design of analogs and CXC chemokine hybrids
    • Clark-Lewis, I., Dewald, B., Loetscher, M., Moser, B. and Baggiolini, M. (1994) Structural requirements for interleukin-8 function identified by design of analogs and CXC chemokine hybrids. J. Biol. Chem. 269, 16075-16081
    • (1994) J. Biol. Chem , vol.269 , pp. 16075-16081
    • Clark-Lewis, I.1    Dewald, B.2    Loetscher, M.3    Moser, B.4    Baggiolini, M.5
  • 8
    • 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. and 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
  • 9
    • 0027516840 scopus 로고
    • Platelet factor 4 binds to interleukin 8 receptors and activates neutrophils when its N terminus is modified with Glu-Leu-Arg
    • Clark-Lewis, I., Dewald, B., Geiser, T., Moser, B. and Baggiolini, M. (1993) Platelet factor 4 binds to interleukin 8 receptors and activates neutrophils when its N terminus is modified with Glu-Leu-Arg. Proc. Natl. Acad. Sci. U.S.A. 90, 3574-3577
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3574-3577
    • Clark-Lewis, I.1    Dewald, B.2    Geiser, T.3    Moser, B.4    Baggiolini, M.5
  • 10
    • 0026559003 scopus 로고
    • IP-10, a γ-interferon-inducible protein related to interleukin-8, lacks neutrophil activating properties
    • Dewald, B., Moser, B., Barella, L., Schumacher, C., Baggiolini, M. and Clark-Lewis, I. (1992) IP-10, a γ -interferon-inducible protein related to interleukin-8, lacks neutrophil activating properties. Immunol. Lett. 32, 81-84
    • (1992) Immunol. Lett , vol.32 , pp. 81-84
    • Dewald, B.1    Moser, B.2    Barella, L.3    Schumacher, C.4    Baggiolini, M.5    Clark-Lewis, I.6
  • 11
    • 0032824805 scopus 로고    scopus 로고
    • Folding funnels and binding mechanisms
    • Ma, B., Kumar, S., Tsai, C. J. and Nussinov, R. (1999) Folding funnels and binding mechanisms. Protein Eng. 12, 713-720
    • (1999) Protein Eng , vol.12 , pp. 713-720
    • Ma, B.1    Kumar, S.2    Tsai, C.J.3    Nussinov, R.4
  • 12
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai, C. J., Kumar, S., Ma, B. and Nussinov, R. (1999) Folding funnels, binding funnels, and protein function. Protein Sci. 8, 1181-1190
    • (1999) Protein Sci , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 13
    • 33845599535 scopus 로고    scopus 로고
    • Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain
    • Fernando, H., Nagle, G. T. and 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
  • 15
    • 3142779910 scopus 로고    scopus 로고
    • Ligand selectivity and affinity of chemokine receptor CXCR1. Role of N-terminal domain
    • Rajagopalan, L. and 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
  • 17
    • 0032508720 scopus 로고    scopus 로고
    • Differential cross-regulation of the human chemokine receptors CXCR1 and CXCR2. Evidence for time-dependent signal generation
    • Richardson, R. M., Pridgen, B. C., Haribabu, B., Ali, H. and Snyderman, R. (1998) Differential cross-regulation of the human chemokine receptors CXCR1 and CXCR2. Evidence for time-dependent signal generation. J. Biol. Chem. 273, 23830-23836
    • (1998) J. Biol. Chem , vol.273 , pp. 23830-23836
    • Richardson, R.M.1    Pridgen, B.C.2    Haribabu, B.3    Ali, H.4    Snyderman, R.5
  • 18
    • 18944394203 scopus 로고    scopus 로고
    • Cross-desensitization among CXCR1, CXCR2, and CCR5: Role of protein kinase C-ε
    • Nasser, M. W., Marjoram, R. J., Brown, S. L. and Richardson, R. M. (2005) Cross-desensitization among CXCR1, CXCR2, and CCR5: role of protein kinase C-ε. J. Immunol. 174, 6927-6933
    • (2005) J. Immunol , vol.174 , pp. 6927-6933
    • Nasser, M.W.1    Marjoram, R.J.2    Brown, S.L.3    Richardson, R.M.4
  • 19
    • 84856413410 scopus 로고    scopus 로고
    • The monomer-dimer equilibrium and glycosaminoglycan interactions of chemokine CXCL8 regulate tissue-specific neutrophil recruitment
    • Gangavarapu, P., Rajagopalan, L., Kolli, D., Guerrero-Plata, A., Garofalo, R. P. and Rajarathnam, K. (2012) The monomer-dimer equilibrium and glycosaminoglycan interactions of chemokine CXCL8 regulate tissue-specific neutrophil recruitment. J. Leukocyte Biol. 91, 259-265
    • (2012) J. Leukocyte Biol , vol.91 , pp. 259-265
    • Gangavarapu, P.1    Rajagopalan, L.2    Kolli, D.3    Guerrero-Plata, A.4    Garofalo, R.P.5    Rajarathnam, K.6
  • 20
    • 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, P. R. and 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
  • 22
    • 17844406393 scopus 로고    scopus 로고
    • Large-scale conformational dynamics of the HIV-1 integrase core domain and its catalytic loop mutants
    • Lee, M. C., Deng, J., Briggs, J. M. and Duan, Y. (2005) Large-scale conformational dynamics of the HIV-1 integrase core domain and its catalytic loop mutants. Biophys. J. 88, 3133-3146
    • (2005) Biophys. J , vol.88 , pp. 3133-3146
    • Lee, M.C.1    Deng, J.2    Briggs, J.M.3    Duan, Y.4
  • 24
    • 77956530120 scopus 로고    scopus 로고
    • Probing the role of CXC motif in chemokine CXCL8 for high affinity binding and activation of CXCR1 and CXCR2 receptors
    • Joseph, P. R., Sarmiento, J. M., Mishra, A. K., Das, S. T., Garofalo, R. P., Navarro, J. and Rajarathnam, K. (2010) Probing the role of CXC motif in chemokine CXCL8 for high affinity binding and activation of CXCR1 and CXCR2 receptors. J. Biol. Chem. 285, 29262-29269
    • (2010) J. Biol. Chem , vol.285 , pp. 29262-29269
    • Joseph, P.R.1    Sarmiento, J.M.2    Mishra, A.K.3    Das, S.T.4    Garofalo, R.P.5    Navarro, J.6    Rajarathnam, K.7
  • 25
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turn in proteins
    • Wilmot, C. M. and Thornton, J. M. (1988) Analysis and prediction of the different types of β-turn in proteins. J. Mol. Biol. 203, 221-232
    • (1988) J. Mol. Biol , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 28
    • 0028971068 scopus 로고
    • 1H NMR solution structure of an active monomeric interleukin-8
    • Rajarathnam, K., Clark-Lewis, I. and Sykes, B. D. (1995) 1H NMR solution structure of an active monomeric interleukin-8. Biochemistry 34, 12983-12990
    • (1995) Biochemistry , vol.34 , pp. 12983-12990
    • Rajarathnam, K.1    Clark-Lewis, I.2    Sykes, B.D.3
  • 30
  • 31
    • 47749148374 scopus 로고    scopus 로고
    • A new protocol for high-yield purification of recombinant human CXCL8(3-72)K11R/G31P expressed in Escherichia coli
    • Cheng, H. T., Huang, K. C., Yu, H. Y., Gao, K. J., Zhao, X., Li, F., Town, J., Gordon, J. R. and Cheng, J. W. (2008) A new protocol for high-yield purification of recombinant human CXCL8(3-72)K11R/G31P expressed in Escherichia coli. Protein Expression Purif. 61, 65-72
    • (2008) Protein Expression Purif , vol.61 , pp. 65-72
    • Cheng, H.T.1    Huang, K.C.2    Yu, H.Y.3    Gao, K.J.4    Zhao, X.5    Li, F.6    Town, J.7    Gordon, J.R.8    Cheng, J.W.9
  • 33
    • 0037126208 scopus 로고    scopus 로고
    • Phylogenetic analysis of 277 human G-protein-coupled receptors as a tool for the prediction of orphan receptor ligands
    • Joost, P. and Methner, A. (2002) Phylogenetic analysis of 277 human G-protein-coupled receptors as a tool for the prediction of orphan receptor ligands. Genome Biol. 3, RESEARCH0063
    • (2002) Genome Biol , vol.3
    • Joost, P.1    Methner, A.2
  • 35
    • 0036295256 scopus 로고    scopus 로고
    • CXCL8(3-73)K11R/G31P antagonizes ligand binding to the neutrophil CXCR1 and CXCR2 receptors and cellular responses to CXCL8/IL-8
    • Li, F., Zhang, X. and Gordon, J. R. (2002) CXCL8(3-73)K11R/G31P antagonizes ligand binding to the neutrophil CXCR1 and CXCR2 receptors and cellular responses to CXCL8/IL-8. Biochem. Biophys. Res. Commun. 293, 939-944
    • (2002) Biochem. Biophys. Res. Commun , vol.293 , pp. 939-944
    • Li, F.1    Zhang, X.2    Gordon, J.R.3
  • 36
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., Sligar, S. G. and Wolynes, P. G. (1991) The energy landscapes and motions of proteins. Science 254, 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 37
    • 60649109828 scopus 로고    scopus 로고
    • Protein allostery, signal transmission and dynamics: A classification scheme of allosteric mechanisms
    • Tsai, C. J., Del Sol, A. and Nussinov, R. (2009) Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms. Mol. BioSys. 5, 207-216
    • (2009) Mol. BioSys , vol.5 , pp. 207-216
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 38
    • 41149104308 scopus 로고    scopus 로고
    • Allostery: Absence of a change in shape does not imply that allostery is not at play
    • Tsai, C. J., del Sol, A. and Nussinov, R. (2008) Allostery: absence of a change in shape does not imply that allostery is not at play. J. Mol. Biol. 378, 1-11
    • (2008) J. Mol. Biol , vol.378 , pp. 1-11
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 39
    • 68149157248 scopus 로고    scopus 로고
    • The origin of allosteric functional modulation: Multiple pre-existing pathways
    • del Sol, A., Tsai, C. J., Ma, B. and Nussinov, R. (2009) The origin of allosteric functional modulation: multiple pre-existing pathways. Structure 17, 1042-1050
    • (2009) Structure , vol.17 , pp. 1042-1050
    • Del Sol, A.1    Tsai, C.J.2    Ma, B.3    Nussinov, R.4
  • 40
    • 77949853850 scopus 로고    scopus 로고
    • Why does binding of proteins to DNA or proteins to proteins not necessarily spell function?
    • Ma, B., Tsai, C. J., Pan, Y. and Nussinov, R. (2010) Why does binding of proteins to DNA or proteins to proteins not necessarily spell function? ACS Chem. Biol. 5, 265-272
    • (2010) ACS Chem. Biol , vol.5 , pp. 265-272
    • Ma, B.1    Tsai, C.J.2    Pan, Y.3    Nussinov, R.4
  • 41
    • 0036147568 scopus 로고    scopus 로고
    • Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations
    • Ma, B., Shatsky, M., Wolfson, H. J. and Nussinov, R. (2002) Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations. Protein Sci. 11, 184-197
    • (2002) Protein Sci , vol.11 , pp. 184-197
    • Ma, B.1    Shatsky, M.2    Wolfson, H.J.3    Nussinov, R.4
  • 43
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr, D. D., McElheny, D., Dyson, H. J. and Wright, P. E. (2006) The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313, 1638-1642
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 45
    • 84856231062 scopus 로고    scopus 로고
    • Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations
    • Qin, H., Lim, L. and Song, J. (2012) Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations. BMC Biophys. 5, 2
    • (2012) BMC Biophys , vol.5 , pp. 2
    • Qin, H.1    Lim, L.2    Song, J.3
  • 46
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: An extended view of binding events
    • Csermely, P., Palotai, R. and Nussinov, R. (2010) Induced fit, conformational selection and independent dynamic segments: an extended view of binding events. Trends Biochem. Sci. 35, 539-546
    • (2010) Trends Biochem. Sci , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 47
    • 84856078561 scopus 로고    scopus 로고
    • Protein dynamics and conformational selection in bidirectional signal transduction
    • Nussinov, R. and Ma, B. (2012) Protein dynamics and conformational selection in bidirectional signal transduction. BMC Biol. 10, 2
    • (2012) BMC Biol , vol.10 , pp. 2
    • Nussinov, R.1    Ma, B.2
  • 48
    • 0033564890 scopus 로고    scopus 로고
    • Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: Dissociation of roles in structure from function
    • Rajarathnam, K., Sykes, B. D., Dewald, B., Baggiolini, M. and Clark-Lewis, I. (1999) Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: dissociation of roles in structure from function. Biochemistry 38, 7653-7658
    • (1999) Biochemistry , vol.38 , pp. 7653-7658
    • Rajarathnam, K.1    Sykes, B.D.2    Dewald, B.3    Baggiolini, M.4    Clark-Lewis, I.5
  • 49
    • 34548713512 scopus 로고    scopus 로고
    • Role of intramolecular disulfides in stability and structure of a noncovalent homodimer
    • Rajagopalan, L., Chin, C. C. and Rajarathnam, K. (2007) Role of intramolecular disulfides in stability and structure of a noncovalent homodimer. Biophys. J. 93, 2129-2134
    • (2007) Biophys. J , vol.93 , pp. 2129-2134
    • Rajagopalan, L.1    Chin, C.C.2    Rajarathnam, K.3
  • 50
    • 0026035103 scopus 로고
    • Comparison of the solution nuclear magnetic resonance and crystal structures of interleukin-8. Possible implications for the mechanism of receptor binding
    • Clore, G. M. and Gronenborn, A. M. (1991) Comparison of the solution nuclear magnetic resonance and crystal structures of interleukin-8. Possible implications for the mechanism of receptor binding. J. Mol. Biol. 217, 611-620
    • (1991) J. Mol. Biol , vol.217 , pp. 611-620
    • Clore, G.M.1    Gronenborn, A.M.2
  • 51
    • 0027193769 scopus 로고
    • Analysis of the backbone dynamics of interleukin-8 by 15N relaxation measurements
    • Grasberger, B. L., Gronenborn, A. M. and Clore, G. M. (1993) Analysis of the backbone dynamics of interleukin-8 by 15N relaxation measurements. J. Mol. Biol. 230, 364-372
    • (1993) J. Mol. Biol , vol.230 , pp. 364-372
    • Grasberger, B.L.1    Gronenborn, A.M.2    Clore, G.M.3
  • 52
    • 0029022355 scopus 로고
    • Conformational variability of solution nuclear magnetic resonance structures
    • Bonvin, A. M. and Brunger, A. T. (1995) Conformational variability of solution nuclear magnetic resonance structures. J. Mol. Biol. 250, 80-93
    • (1995) J. Mol. Biol , vol.250 , pp. 80-93
    • Bonvin, A.M.1    Brunger, A.T.2
  • 54
    • 0033081379 scopus 로고    scopus 로고
    • Structure of a CXC chemoline-receptor fragment in complex with interleukin-8
    • Skelton, N. J., Quan, C., Reilly, D. and Lowman, H. (1999) Structure of a CXC chemoline-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
  • 55
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka, B. K. and Deupi, X. (2007) Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28, 397-406
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 56
    • 78149496656 scopus 로고    scopus 로고
    • The role of conformational ensembles of seven transmembrane receptors in functional selectivity
    • Vaidehi, N. and Kenakin, T. (2010) The role of conformational ensembles of seven transmembrane receptors in functional selectivity. Curr. Opin. Pharmacol. 10, 775-781
    • (2010) Curr. Opin. Pharmacol , vol.10 , pp. 775-781
    • Vaidehi, N.1    Kenakin, T.2
  • 57
    • 17644413780 scopus 로고    scopus 로고
    • Water and molecular chaperones act as weak links of protein folding networks: Energy landscape and punctuated equilibrium changes point towards a game theory of proteins
    • Kovacs, I. A., Szalay, M. S. and Csermely, P. (2005) Water and molecular chaperones act as weak links of protein folding networks: energy landscape and punctuated equilibrium changes point towards a game theory of proteins. FEBS Lett. 579, 2254-2260
    • (2005) FEBS Lett , vol.579 , pp. 2254-2260
    • Kovacs, I.A.1    Szalay, M.S.2    Csermely, P.3
  • 58
    • 65649138753 scopus 로고    scopus 로고
    • Perturbation waves in proteins and protein networks: Applications of percolation and game theories in signaling and drug design
    • Antal, M. A., Bode, C. and Csermely, P. (2009) Perturbation waves in proteins and protein networks: applications of percolation and game theories in signaling and drug design. Curr. Protein Pept. Sci. 10, 161-172
    • (2009) Curr. Protein Pept. Sci , vol.10 , pp. 161-172
    • Antal, M.A.1    Bode, C.2    Csermely, P.3
  • 60
    • 0031028162 scopus 로고    scopus 로고
    • Neutrophil-activating peptide-2 and melanoma growth-stimulatory activity are functional as monomers for neutrophil activation
    • Rajarathnam, K., Kay, C. M., Dewald, B., Wolf, M., Baggiolini, M., Clark-Lewis, I. and Sykes, B. D. (1997) Neutrophil-activating peptide-2 and melanoma growth-stimulatory activity are functional as monomers for neutrophil activation. J. Biol. Chem. 272, 1725-1729
    • (1997) J. Biol. Chem , vol.272 , pp. 1725-1729
    • Rajarathnam, K.1    Kay, C.M.2    Dewald, B.3    Wolf, M.4    Baggiolini, M.5    Clark-Lewis, I.6    Sykes, B.D.7
  • 62
    • 33745037748 scopus 로고    scopus 로고
    • Reply to 'A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation'
    • Rajarathnam, K. (2006) Reply to 'A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation'. Nat. Med. 12, 603-604
    • (2006) Nat. Med , vol.12 , pp. 603-604
    • Rajarathnam, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.