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Volumn 274, Issue 1, 2007, Pages 241-251

Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain

Author keywords

Interleukin 8; Isothermal titration calorimetry; Monomer; N terminal domain; Thermodynamics

Indexed keywords

CHEMOKINE RECEPTOR CXCR1; INTERLEUKIN 8; MONOMER; TRIMETHYLAMINE;

EID: 33845599535     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05579.x     Document Type: Article
Times cited : (38)

References (48)
  • 1
    • 0036467505 scopus 로고    scopus 로고
    • The role of chemokines in linking innate and adaptive immunity
    • Luster AD (2002) The role of chemokines in linking innate and adaptive immunity. Curr Opin Immunol 14, 129-135.
    • (2002) Curr Opin Immunol , vol.14 , pp. 129-135
    • Luster, A.D.1
  • 2
    • 0842324615 scopus 로고    scopus 로고
    • Chemokines: Multiple levels of leukocyte migration control
    • Moser B, Wolf M, Walz A & Loetscher P (2004) Chemokines: multiple levels of leukocyte migration control. Trends Immunol 25, 75-84.
    • (2004) Trends Immunol , vol.25 , pp. 75-84
    • Moser, B.1    Wolf, M.2    Walz, A.3    Loetscher, P.4
  • 3
    • 0034969031 scopus 로고    scopus 로고
    • Agonistic and antagonistic activities of chemokines
    • Loetscher P & Clark-Lewis I (2001) Agonistic and antagonistic activities of chemokines. J Leukoc Biol 69, 881-884.
    • (2001) J Leukoc Biol , vol.69 , pp. 881-884
    • Loetscher, P.1    Clark-Lewis, I.2
  • 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
    • 0030683638 scopus 로고    scopus 로고
    • Solution structure and basis for functional activity of stromal derived cell-derived factor-1: Dissociation of CXCR4 activation from binding and inhibition of HIV-1
    • Crump MP, Gong JH, Loetscher P, Rajarathnam K, Arenzana-Seisdedos F, Virelizier J-L, Baggiolini M, Sykes BD & Clark-Lewis I (1997) Solution structure and basis for functional activity of stromal derived cell-derived factor-1: dissociation of CXCR4 activation from binding and inhibition of HIV-1. EMBO J 16, 6996-7007.
    • (1997) EMBO J , vol.16 , pp. 6996-7007
    • Crump, M.P.1    Gong, J.H.2    Loetscher, P.3    Rajarathnam, K.4    Arenzana-Seisdedos, F.5    Virelizier, J.-L.6    Baggiolini, M.7    Sykes, B.D.8    Clark-Lewis, I.9
  • 6
    • 0030816336 scopus 로고    scopus 로고
    • Neutrophil receptors for interleukin-8 and related CXC chemokines
    • Murphy PM (1997) Neutrophil receptors for interleukin-8 and related CXC chemokines. Semin Hematol 34, 311-318.
    • (1997) Semin Hematol , vol.34 , pp. 311-318
    • Murphy, P.M.1
  • 7
    • 9444267059 scopus 로고    scopus 로고
    • The CXC chemokines growth-regulated oncogene (GRO) α, GROβ, GROγ, neutrophil-activating peptide-2, and epithelial cellderived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor
    • Ahuja SK & Murphy PM (1996) The CXC chemokines growth-regulated oncogene (GRO) α, GROβ, GROγ, neutrophil-activating peptide-2, and epithelial cellderived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor. J Biol Chem 271, 20545-20550.
    • (1996) J Biol Chem , vol.271 , pp. 20545-20550
    • Ahuja, S.K.1    Murphy, P.M.2
  • 11
    • 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
    • 0028305217 scopus 로고
    • Structural requirements for IL-8 function identified by design of analogs and CXC chemokine hybrids
    • Clark-Lewis I, Dewald B, Loetscher M, Moser B & Baggiolini M (1994) Structural requirements for IL-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
  • 14
    • 0033564890 scopus 로고    scopus 로고
    • Disulfide bridges in interleukin-8 probed using non-natural disulfide analogs: Dissociation of roles in structure and function
    • Rajarathnam K, Dewald B, Baggiolini M, Sykes BD & Clark-Lewis I (1999) Disulfide bridges in interleukin-8 probed using non-natural disulfide analogs: dissociation of roles in structure and function. Biochemistry 38, 7653-7658.
    • (1999) Biochemistry , vol.38 , pp. 7653-7658
    • Rajarathnam, K.1    Dewald, B.2    Baggiolini, M.3    Sykes, B.D.4    Clark-Lewis, I.5
  • 15
    • 0028178519 scopus 로고
    • 1H NMR studies of interleukin-8 analogs: Characterization of the domains essential for function
    • 1H NMR studies of interleukin-8 analogs: characterization of the domains essential for function. Biochemistry 33, 6623-6630.
    • (1994) Biochemistry , vol.33 , pp. 6623-6630
    • Rajarathnam, K.1    Clark-Lewis, I.2    Sykes, B.D.3
  • 16
    • 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
  • 17
    • 0033597253 scopus 로고    scopus 로고
    • Differential mechanisms of recognition and activation of interleukin-8 receptor subtypes
    • Suetomi K, Lu Z, Heck T, Wood TG, Prusak DJ, Dunn KJ & Navarro J (1999) Differential mechanisms of recognition and activation of interleukin-8 receptor subtypes. J Biol Chem 274, 11768-11772.
    • (1999) J Biol Chem , vol.274 , pp. 11768-11772
    • Suetomi, K.1    Lu, Z.2    Heck, T.3    Wood, T.G.4    Prusak, D.J.5    Dunn, K.J.6    Navarro, J.7
  • 18
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors. I. Diversity of receptor-ligand interactions
    • Ji TH, Grossmann M & Ji I (1998) G protein-coupled receptors. I. Diversity of receptor-ligand interactions. J Biol Chem 273, 17299-17302.
    • (1998) J Biol Chem , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.3
  • 19
    • 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
  • 22
    • 4344589888 scopus 로고    scopus 로고
    • Dimer dissociation is essential for interleukin-8 (IL-8) binding to CXCR1 receptor
    • Fernando H, Chin C, Rösgen 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    Rösgen, J.3    Rajarathnam, K.4
  • 23
    • 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
  • 24
    • 25444533030 scopus 로고    scopus 로고
    • Novel use of an osmolyte to dissect thermodynamic linkages between receptor N-domain folding, ligand binding, and ligand dimerization in a chemokine-receptor system
    • Rajagopalan L, Rösgen J, Bolen DW & Rajarathnam K (2005) Novel use of an osmolyte to dissect thermodynamic linkages between receptor N-domain folding, ligand binding, and ligand dimerization in a chemokine-receptor system. Biochemistry 44, 12932-12939.
    • (2005) Biochemistry , vol.44 , pp. 12932-12939
    • Rajagopalan, L.1    Rösgen, J.2    Bolen, D.W.3    Rajarathnam, K.4
  • 25
    • 33746901672 scopus 로고    scopus 로고
    • Probing receptor binding activity of interleukin-8 dimer using a disulfide trap
    • Rajarathnam K, Prado GN, Fernando H, Clark-Lewis I & Navarro J (2006) Probing receptor binding activity of interleukin-8 dimer using a disulfide trap. Biochemistry 45, 7882-7888.
    • (2006) Biochemistry , vol.45 , pp. 7882-7888
    • Rajarathnam, K.1    Prado, G.N.2    Fernando, H.3    Clark-Lewis, I.4    Navarro, J.5
  • 26
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt S & Freire E (2001) Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr Opin Struct Biol 11, 560-566.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 27
    • 0034282648 scopus 로고    scopus 로고
    • Characterization of binding between the chemokine eotaxin and peptides derived from the chemokine receptor CCR3
    • Ye J, Kohli LL & Stone MJ (2000) Characterization of binding between the chemokine eotaxin and peptides derived from the chemokine receptor CCR3. J Biol Chem 275, 27250-27257.
    • (2000) J Biol Chem , vol.275 , pp. 27250-27257
    • Ye, J.1    Kohli, L.L.2    Stone, M.J.3
  • 28
    • 0034713909 scopus 로고    scopus 로고
    • NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2
    • Mayer KL & Stone MJ (2000) NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2. Biochemistry 39, 8382-8395.
    • (2000) Biochemistry , vol.39 , pp. 8382-8395
    • Mayer, K.L.1    Stone, M.J.2
  • 29
    • 0037143532 scopus 로고    scopus 로고
    • The CXCR3 binding chemokine IP-10/CXCL10: Structure and receptor interactions
    • Booth V, Keizer DW, Kamphuis MB, Clark-Lewis I & Sykes BD (2002) The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions. Biochemistry 41, 10418-10425.
    • (2002) Biochemistry , vol.41 , pp. 10418-10425
    • Booth, V.1    Keizer, D.W.2    Kamphuis, M.B.3    Clark-Lewis, I.4    Sykes, B.D.5
  • 31
    • 0040560068 scopus 로고    scopus 로고
    • Solution structure and dynamics of the CX3C chemokine domain of fractalkine and its interaction with an N-terminal fragment of CX3CR1
    • Mizoue LS, Bazan JF, Johnson EC & Handel TM (1999) Solution structure and dynamics of the CX3C chemokine domain of fractalkine and its interaction with an N-terminal fragment of CX3CR1. Biochemistry 38, 1402-1414.
    • (1999) Biochemistry , vol.38 , pp. 1402-1414
    • Mizoue, L.S.1    Bazan, J.F.2    Johnson, E.C.3    Handel, T.M.4
  • 33
    • 0030625187 scopus 로고    scopus 로고
    • Characterization of quaternary structure of interleukin-8 and functional implications
    • Rajarathnam K, Kay CM, Clark-Lewis I & Sykes BD (1997) Characterization of quaternary structure of interleukin-8 and functional implications. Methods Enzymol 287, 89-105.
    • (1997) Methods Enzymol , vol.287 , pp. 89-105
    • Rajarathnam, K.1    Kay, C.M.2    Clark-Lewis, I.3    Sykes, B.D.4
  • 34
    • 0026333179 scopus 로고
    • Structure-activity relationship of interleukin-8 determined using chemically synthesized analogs
    • Clark-Lewis I, Schumacher C, Baggiolini M & Moser B (1991) Structure-activity relationship of interleukin-8 determined using chemically synthesized analogs. 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
  • 36
    • 0028988191 scopus 로고
    • The role of Tyr13 and Lys15 of interleukin-8 in the high affinity interaction with the interleukin-8 receptor type A
    • Schraufstatter IU, Ma M, Oades ZG, Barritt DS & Cochrane CG (1995) The role of Tyr13 and Lys15 of interleukin-8 in the high affinity interaction with the interleukin-8 receptor type A. J Biol Chem 270, 10428-10431.
    • (1995) J Biol Chem , vol.270 , pp. 10428-10431
    • Schraufstatter, I.U.1    Ma, M.2    Oades, Z.G.3    Barritt, D.S.4    Cochrane, C.G.5
  • 37
    • 0027293058 scopus 로고
    • Partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain
    • (erratum appears in J Biol Chem 269, 16520)
    • Hébert CA, Chuntharapai A, Smith M, Colby T, Kim J & Horuk R (1993) Partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain. J Biol Chem 268, 18549-18553 (erratum appears in J Biol Chem 269, 16520).
    • (1993) J Biol Chem , vol.268 , pp. 18549-18553
    • Hébert, C.A.1    Chuntharapai, A.2    Smith, M.3    Colby, T.4    Kim, J.5    Horuk, R.6
  • 38
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker BM & Murphy KP (1996) Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys J 71, 2049-2055.
    • (1996) Biophys J , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 39
    • 24044470332 scopus 로고    scopus 로고
    • Angiogenesis and rhodopsin-like receptors: A role for N-terminal acidic residues?
    • Parker SL, Parker MS, Sah R & Sallee F (2005) Angiogenesis and rhodopsin-like receptors: a role for N-terminal acidic residues? Biochem Biophys Res Commun 335, 983-992.
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 983-992
    • Parker, S.L.1    Parker, M.S.2    Sah, R.3    Sallee, F.4
  • 42
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand AJ (2001) Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nat Struct Biol 8, 926-931.
    • (2001) Nat Struct Biol , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 43
    • 33646911358 scopus 로고    scopus 로고
    • Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
    • Jarymowycz VA & Stone MJ (2006) Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chem Rev 106, 1624-1671.
    • (2006) Chem Rev , vol.106 , pp. 1624-1671
    • Jarymowycz, V.A.1    Stone, M.J.2
  • 44
    • 0032710610 scopus 로고    scopus 로고
    • Increased protein backbone conformational entropy upon hydrophobic ligand binding
    • Zidek L, Novotony MV & Stone MJ (1999) Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nat Struct Biol 6, 1118-1121.
    • (1999) Nat Struct Biol , vol.6 , pp. 1118-1121
    • Zidek, L.1    Novotony, M.V.2    Stone, M.J.3
  • 45
    • 0027537127 scopus 로고
    • Structural energetics of peptide recognition: Angiotensin II/antibody binding
    • Murphy KP, Xie D, Garcia KC, Amzel LM & Freire E (1993) Structural energetics of peptide recognition: angiotensin II/antibody binding. Proteins 15, 113-120.
    • (1993) Proteins , vol.15 , pp. 113-120
    • Murphy, K.P.1    Xie, D.2    Garcia, K.C.3    Amzel, L.M.4    Freire, E.5
  • 46
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen DW & Baskakov IV (2001) The osmophobic effect: natural selection of a thermodynamic force in protein folding. J Mol Biol 310, 955-963.
    • (2001) J Mol Biol , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 47
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy KP & Freire E (1992) Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem 43, 313-361.
    • (1992) Adv Protein Chem , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 48
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T, Williston S, Brandts JF & Lin LN (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179, 131-137.
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4


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