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Volumn 26, Issue 5, 2006, Pages 325-339

Structural basis of chemokine receptor function - A model for binding affinity and ligand selectivity

Author keywords

Binding affinity; Chemokine; Chemokine receptor; GPCR; N terminal domain; Receptor activation structure function; Selectivity

Indexed keywords

CHEMOKINE RECEPTOR; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR1; CHEMOKINE RECEPTOR CXCR2; CHEMOKINE RECEPTOR CXCR3; CHEMOKINE RECEPTOR CXCR4; CHEMOKINE RECEPTOR CXCR5; CHEMOKINE RECEPTOR CXCR6; G PROTEIN COUPLED RECEPTOR; GAG PROTEIN; INTERLEUKIN 8; RANTES;

EID: 33750929921     PISSN: 01448463     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10540-006-9025-9     Document Type: Review
Times cited : (117)

References (103)
  • 1
    • 0030022829 scopus 로고    scopus 로고
    • CXC chemokines bind to unique sets of selectivity determinants that can function independently and are broadly distributed on multiple domains of human interleukin-8 receptor B. Determinants of high affinity binding and receptor activation are distinct
    • Ahuja SK, Lee JC, Murphy PM (1996) CXC chemokines bind to unique sets of selectivity determinants that can function independently and are broadly distributed on multiple domains of human interleukin-8 receptor B. Determinants of high affinity binding and receptor activation are distinct. J Biol Chem 271:225-232
    • (1996) J Biol Chem , vol.271 , pp. 225-232
    • Ahuja, S.K.1    Lee, J.C.2    Murphy, P.M.3
  • 2
    • 9444267059 scopus 로고    scopus 로고
    • The CXC chemokines growth-regulated oncogene (GRO)α, GROβ, GROγ, Neutrophil-activating peptide-2, and epithelial cell-dervived 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 cell-dervived 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
  • 3
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • Alcami A (2003) Viral mimicry of cytokines, chemokines and their receptors. Nat Rev Immunol 3:36-50
    • (2003) Nat Rev Immunol , vol.3 , pp. 36-50
    • Alcami, A.1
  • 4
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G proteins
    • Baldwin JM (1994) Structure and function of receptors coupled to G proteins. Curr Opin Cell Biol 6:180-190
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 180-190
    • Baldwin, J.M.1
  • 5
    • 0141679065 scopus 로고    scopus 로고
    • Oligomerization of RANTES is required for CCR1-mediated arrest but not CCR5-mediated transmigration of leukocytes on inflamed endothelium
    • Baltus T, Weber KS, Johnson Z, Proudfoot AE, Weber C (2003) Oligomerization of RANTES is required for CCR1-mediated arrest but not CCR5-mediated transmigration of leukocytes on inflamed endothelium. Blood 102:1985-1988
    • (2003) Blood , vol.102 , pp. 1985-1988
    • Baltus, T.1    Weber, K.S.2    Johnson, Z.3    Proudfoot, A.E.4    Weber, C.5
  • 7
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine Receptors as HIV-1 Coreceptors: Roles in viral entry, tropism, and disease
    • Berger EA, Murphy PM, Farber JM (1999) Chemokine Receptors as HIV-1 Coreceptors: roles in viral entry, tropism, and disease. Annu Rev Immunol 17:657-700
    • (1999) Annu Rev Immunol , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 11
    • 0037137183 scopus 로고    scopus 로고
    • Characterization of the role of the N-loop of MIP-1 beta in CCR5 binding
    • Bondue A, Jao SC, Blanpain C, Parmentier M, LiWang PJ (2002) Characterization of the role of the N-loop of MIP-1 beta in CCR5 binding. Biochemistry 41:13548-13555
    • (2002) Biochemistry , vol.41 , pp. 13548-13555
    • Bondue, A.1    Jao, S.C.2    Blanpain, C.3    Parmentier, M.4    Liwang, P.J.5
  • 12
    • 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
  • 13
    • 0034604709 scopus 로고    scopus 로고
    • Identification of residues of CXCR4 critical for human immunodeficiency virus coreceptor and chemokine receptor activities
    • Brelot A, Heveker N, Montes M, Alizon M (2000) Identification of residues of CXCR4 critical for human immunodeficiency virus coreceptor and chemokine receptor activities. J Biol Chem 275:23736-23744
    • (2000) J Biol Chem , vol.275 , pp. 23736-23744
    • Brelot, A.1    Heveker, N.2    Montes, M.3    Alizon, M.4
  • 14
    • 0038608022 scopus 로고    scopus 로고
    • CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10)
    • Campanella GS, Lee EM, Sun J, Luster AD (2003) CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10). J Biol Chem 278:17066-17074
    • (2003) J Biol Chem , vol.278 , pp. 17066-17074
    • Campanella, G.S.1    Lee, E.M.2    Sun, J.3    Luster, A.D.4
  • 16
    • 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, 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 USA 90:3574-3577
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3574-3577
    • Clark-Lewis, I.1    Dewald, B.2    Geiser, T.3    Moser, B.4    Baggiolini, M.5
  • 17
    • 0028305217 scopus 로고
    • Structural requirements for IL8 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 IL8 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
  • 19
    • 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
  • 21
    • 0034705106 scopus 로고    scopus 로고
    • Specific interaction of CCR5 amino-terminal domain peptides containing sulfotyrosines with HIV-1 envelope glycoprotein gp120
    • Cormier EG, Persuh M, Thompson DA, Lin SW, Sakmar TP, Olson WC, Dragic T (2000) Specific interaction of CCR5 amino-terminal domain peptides containing sulfotyrosines with HIV-1 envelope glycoprotein gp120. Proc Natl Acad Sci USA 97:5762-5767
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5762-5767
    • Cormier, E.G.1    Persuh, M.2    Thompson, D.A.3    Lin, S.W.4    Sakmar, T.P.5    Olson, W.C.6    Dragic, T.7
  • 23
    • 0032575660 scopus 로고    scopus 로고
    • Solution structure of eotaxin: A chemokine that selectively recruits eosinophils in allergic inflammation
    • Crump M, Rajarathnam K, Kim K-S, Clark-Lewis I, Sykes BD (1998) Solution structure of eotaxin: a chemokine that selectively recruits eosinophils in allergic inflammation. J Biol Chem 273:22471-22479
    • (1998) J Biol Chem , vol.273 , pp. 22471-22479
    • Crump, M.1    Rajarathnam, K.2    Kim, K.-S.3    Clark-Lewis, I.4    Sykes, B.D.5
  • 25
    • 8744306141 scopus 로고    scopus 로고
    • Chemokine-binding specificity of soluble chemokine-receptor analogues: Identification of interacting elements by chimera complementation
    • Datta-Mannan A, Stone MJ (2004) Chemokine-binding specificity of soluble chemokine-receptor analogues: identification of interacting elements by chimera complementation. Biochemistry 43:14602-14611
    • (2004) Biochemistry , vol.43 , pp. 14602-14611
    • Datta-Mannan, A.1    Stone, M.J.2
  • 27
    • 0037119426 scopus 로고    scopus 로고
    • The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry
    • Farzan M, Babcock GJ, Vasilieva N, Wright PL, Kiprilov E, Mirzabekov T, Choe H (2002) The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry. J Biol Chem 277:29484-29489
    • (2002) J Biol Chem , vol.277 , pp. 29484-29489
    • Farzan, M.1    Babcock, G.J.2    Vasilieva, N.3    Wright, P.L.4    Kiprilov, E.5    Mirzabekov, T.6    Choe, H.7
  • 29
    • 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
  • 30
    • 4344589888 scopus 로고    scopus 로고
    • Dimer dissociation is essential for interleukin-8 (IL8) binding to CXCR1 receptor
    • Fernando H, Chin C, Rösgen J, Rajarathnam K (2004) Dimer dissociation is essential for interleukin-8 (IL8) 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
  • 31
    • 0037204744 scopus 로고    scopus 로고
    • CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion
    • Fong AM, Alam SM, Imai T, Haribabu B, Patel DD (2002) CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. J Biol Chem 277:19418-19489
    • (2002) J Biol Chem , vol.277 , pp. 19418-19489
    • Fong, A.M.1    Alam, S.M.2    Imai, T.3    Haribabu, B.4    Patel, D.D.5
  • 33
  • 36
    • 0000113237 scopus 로고    scopus 로고
    • Role of the first extracellular loop in the functional activation of CCR2. The first extracellular loop contains distinct domains necessary for both agonist binding and transmembrane signaling
    • Han KH, Green SR, Tangirala RK, Tanaka S, Quehenberger O (1999) Role of the first extracellular loop in the functional activation of CCR2. The first extracellular loop contains distinct domains necessary for both agonist binding and transmembrane signaling. J Biol Chem 274:32055-32062
    • (1999) J Biol Chem , vol.274 , pp. 32055-32062
    • Han, K.H.1    Green, S.R.2    Tangirala, R.K.3    Tanaka, S.4    Quehenberger, O.5
  • 37
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - As exemplified by chemokines
    • Handel TM, Johnson Z, Crown SE, Lau EK, Proudfoot AE (2005) Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu Rev Biochem 74:385-410
    • (2005) Annu Rev Biochem , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 38
    • 0027293058 scopus 로고
    • Partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain
    • Hebert 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
    • (1993) J Biol Chem , vol.268 , pp. 18549-18553
    • Hebert, C.A.1    Chuntharapai, A.2    Smith, M.3    Colby, T.4    Kim, J.5    Horuk, R.6
  • 41
    • 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
  • 43
    • 0033793697 scopus 로고    scopus 로고
    • Interleukin 8:neutrophil-activating peptide-2 and GRO-alpha bind to and elicit cell activation via specific and different amino acid residues of CXCR2
    • Katancik JA, Sharma A, de Nardin E (2000) Interleukin 8:neutrophil-activating peptide-2 and GRO-alpha bind to and elicit cell activation via specific and different amino acid residues of CXCR2. Cytokine 12:1480-1488
    • (2000) Cytokine , vol.12 , pp. 1480-1488
    • Katancik, J.A.1    Sharma, A.2    De Nardin, E.3
  • 44
    • 0028556891 scopus 로고
    • Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy
    • Kim KS, Clark-Lewis I, Sykes BD (1994) Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy. J Biol Chem 269:32909-32915
    • (1994) J Biol Chem , vol.269 , pp. 32909-32915
    • Kim, K.S.1    Clark-Lewis, I.2    Sykes, B.D.3
  • 45
    • 0030597050 scopus 로고    scopus 로고
    • Structural characterization of a monomeric chemokine: Monocyte chemoattractant protein-3
    • Kim KS, Rajarathnam K, Clark-Lewis I, Sykes BD (1996) Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3. FEBS Lett 395:277-282
    • (1996) FEBS Lett , vol.395 , pp. 277-282
    • Kim, K.S.1    Rajarathnam, K.2    Clark-Lewis, I.3    Sykes, B.D.4
  • 46
    • 0033192434 scopus 로고    scopus 로고
    • Evasion and exploitation of chemokines by viruses
    • Lalani AS, McFadden G (1999) Evasion and exploitation of chemokines by viruses. Cytokine Growth Factor Rev 10:219-233
    • (1999) Cytokine Growth Factor Rev , vol.10 , pp. 219-233
    • Lalani, A.S.1    McFadden, G.2
  • 48
    • 16544379697 scopus 로고    scopus 로고
    • Chemokine-receptor interactions: GPCRs, glycosaminoglycans and viral chemokine binding proteins
    • Lau EK, Allen S, Hsu AR, Handel TM (2004) Chemokine-receptor interactions: GPCRs, glycosaminoglycans and viral chemokine binding proteins. Adv Protein Chem 68:351-391
    • (2004) Adv Protein Chem , vol.68 , pp. 351-391
    • Lau, E.K.1    Allen, S.2    Hsu, A.R.3    Handel, T.M.4
  • 49
    • 0034724373 scopus 로고    scopus 로고
    • CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding
    • Laurence JS, Blanpain C, Burgner JW, Parmentier M, LiWang PJ (2000) CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding. Biochemistry 39:3401-3409
    • (2000) Biochemistry , vol.39 , pp. 3401-3409
    • Laurence, J.S.1    Blanpain, C.2    Burgner, J.W.3    Parmentier, M.4    Liwang, P.J.5
  • 50
    • 0035942317 scopus 로고    scopus 로고
    • Importance of basic residues and quaternary structure in the function of MIP-1 beta: CCR5 binding and cell surface sugar interactions
    • Laurence JS, Blanpain C, De Leener A, Parmentier M, LiWang PJ (2001) Importance of basic residues and quaternary structure in the function of MIP-1 beta: CCR5 binding and cell surface sugar interactions. Biochemistry 40:4990-4999
    • (2001) Biochemistry , vol.40 , pp. 4990-4999
    • Laurence, J.S.1    Blanpain, C.2    De Leener, A.3    Parmentier, M.4    LiWang, P.J.5
  • 53
    • 0032575620 scopus 로고    scopus 로고
    • N-terminal peptides of stromal cell-derived factor-1 with CXC chemokine receptor 4 agonist and antagonist activities
    • Loetscher P, Gong JH, Dewald B, Baggiolini M, Clark-Lewis I (1998) N-terminal peptides of stromal cell-derived factor-1 with CXC chemokine receptor 4 agonist and antagonist activities. J Biol Chem 273(35):22279-22283
    • (1998) J Biol Chem , vol.273 , Issue.35 , pp. 22279-22283
    • Loetscher, P.1    Gong, J.H.2    Dewald, B.3    Baggiolini, M.4    Clark-Lewis, I.5
  • 55
    • 0032509889 scopus 로고    scopus 로고
    • Chemokines - Chemotactic cytokines that mediate inflammation
    • Luster AD (1998) Chemokines - chemotactic cytokines that mediate inflammation. N Engl J Med 338:436-445
    • (1998) N Engl J Med , vol.338 , pp. 436-445
    • Luster, A.D.1
  • 56
    • 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 Immunology 14:129-135
    • (2002) Curr Opin Immunology , vol.14 , pp. 129-135
    • Luster, A.D.1
  • 57
    • 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
  • 59
    • 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
  • 60
    • 0029761071 scopus 로고    scopus 로고
    • The amino-terminal extracellular domain of the MCP-1 receptor, but not the RANTES/MIP-1alpha receptor, confers chemokine selectivity. Evidence for a two-step mechanism for MCP-1 receptor activation
    • Monteclaro FS, Charo IF (1996) The amino-terminal extracellular domain of the MCP-1 receptor, but not the RANTES/MIP-1alpha receptor, confers chemokine selectivity. Evidence for a two-step mechanism for MCP-1 receptor activation. J Biol Chem 271:19084-19092
    • (1996) J Biol Chem , vol.271 , pp. 19084-19092
    • Monteclaro, F.S.1    Charo, I.F.2
  • 62
    • 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
  • 63
    • 0035856010 scopus 로고    scopus 로고
    • Chemokines and the molecular basis of cancer metastasis
    • Murphy PM (2001) Chemokines and the molecular basis of cancer metastasis. N Engl J Med 345:833-835
    • (2001) N Engl J Med , vol.345 , pp. 833-835
    • Murphy, P.M.1
  • 66
    • 0037097585 scopus 로고    scopus 로고
    • Cholesterol is essential for macrophage inflammatory protein 1 beta binding and conformational integrity of CC chemokine receptor 5
    • Nguyen DH, Taub D (2002) Cholesterol is essential for macrophage inflammatory protein 1 beta binding and conformational integrity of CC chemokine receptor 5. Blood 99:4298-4306
    • (2002) Blood , vol.99 , pp. 4298-4306
    • Nguyen, D.H.1    Taub, D.2
  • 68
    • 0030811908 scopus 로고    scopus 로고
    • Distinct but overlapping epitopes for the interaction of a CC-chemokine with CCR1, CCR3 and CCR5
    • Pakianathan DR, Kuta EG, Artis DR, Skelton NJ, Hebert CA (1997) Distinct but overlapping epitopes for the interaction of a CC-chemokine with CCR1, CCR3 and CCR5. Biochemistry 36:9642-9648
    • (1997) Biochemistry , vol.36 , pp. 9642-9648
    • Pakianathan, D.R.1    Kuta, E.G.2    Artis, D.R.3    Skelton, N.J.4    Hebert, C.A.5
  • 70
    • 0034327691 scopus 로고    scopus 로고
    • Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region
    • Preobrazhensky AA, Dragan S, Kawano T, Gavrilin MA, Gulina IV, Chakravarty L, Kolattukudy PE (2000) Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region. J Immunol 165:5295-5303
    • (2000) J Immunol , vol.165 , pp. 5295-5303
    • Preobrazhensky, A.A.1    Dragan, S.2    Kawano, T.3    Gavrilin, M.A.4    Gulina, I.V.5    Chakravarty, L.6    Kolattukudy, P.E.7
  • 73
    • 0033579486 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of truncated human GRObeta [5-73] and its structural comparison with CXC chemokine family members GROalpha and IL-8
    • Qian YQ, Johanson KO, McDevitt P (1999) Nuclear magnetic resonance solution structure of truncated human GRObeta [5-73] and its structural comparison with CXC chemokine family members GROalpha and IL-8. J Mol Biol 294:1065-1072
    • (1999) J Mol Biol , vol.294 , pp. 1065-1072
    • Qian, Y.Q.1    Johanson, K.O.2    McDevitt, P.3
  • 74
    • 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
  • 75
    • 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
  • 76
    • 0036400905 scopus 로고    scopus 로고
    • Designing decoys for chemokine-chemokine receptor interaction
    • Rajarathnam K (2002) Designing decoys for chemokine-chemokine receptor interaction. Curr Pharm, Des 8:2159-2169
    • (2002) Curr Pharm, Des , vol.8 , pp. 2159-2169
    • Rajarathnam, K.1
  • 77
    • 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
  • 80
    • 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
  • 81
    • 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
  • 82
    • 0031028162 scopus 로고    scopus 로고
    • Neutrophil activating peptide-2 (NAP-2) and Melanoma growth stimulatory activity (MGSA) are functional as Monomers for Neutrophil activation
    • Rajarathnam K, Kay CM, Dewald B, Wolf M, Baggiolini M, Clark-Lewis I, Sykes BD (1997) Neutrophil activating peptide-2 (NAP-2) and Melanoma growth stimulatory activity (MGSA) 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
  • 83
    • 0035895873 scopus 로고    scopus 로고
    • Solution structure and dynamics of Myeloid progenitor inhibitor factor-1 (MPIF-1): A novel monomeric CC chemokine
    • Rajarathnam K, Li Y, Rohrer T, Gentz R (2001) Solution structure and dynamics of Myeloid progenitor inhibitor factor-1 (MPIF-1): a novel monomeric CC chemokine. J Biol Chem 276:4909-4916
    • (2001) J Biol Chem , vol.276 , pp. 4909-4916
    • Rajarathnam, K.1    Li, Y.2    Rohrer, T.3    Gentz, R.4
  • 86
    • 2142827810 scopus 로고    scopus 로고
    • How do chemokine/chemokine receptor activations affect tumorigenesis?
    • Richmond A, Fan GH, Dhawan P, Yang J (2004) How do chemokine/chemokine receptor activations affect tumorigenesis?. Novartis Found Symp 256:74-89
    • (2004) Novartis Found Symp , vol.256 , pp. 74-89
    • Richmond, A.1    Fan, G.H.2    Dhawan, P.3    Yang, J.4
  • 87
    • 2542428442 scopus 로고    scopus 로고
    • Chemokines in innate and adaptive host defense: Basic chemokinese grammar for immune cells
    • Rot A, von Andrian UH (2004) Chemokines in innate and adaptive host defense: basic chemokinese grammar for immune cells. Annu Rev Immunol 22:891-928
    • (2004) Annu Rev Immunol , vol.22 , pp. 891-928
    • Rot, A.1    Von Andrian, U.H.2
  • 88
    • 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
  • 89
    • 0036973938 scopus 로고    scopus 로고
    • Structural analysis of human CCR2b and primate CCR2b by molecular modeling and molecular dynamics simulation
    • Shi XF, Liu S, Xiangyu J, Zhang Y, Huang J, Liu S, Liu CQ (2002) Structural analysis of human CCR2b and primate CCR2b by molecular modeling and molecular dynamics simulation. J Mol Model (Online) 7:217-222
    • (2002) J Mol Model (Online) , vol.7 , pp. 217-222
    • Shi, X.F.1    Liu, S.2    Xiangyu, J.3    Zhang, Y.4    Huang, J.5    Liu, S.6    Liu, C.Q.7
  • 90
    • 0036878155 scopus 로고    scopus 로고
    • N-terminal domain of eotaxin-3 is important for activation of CC chemokine receptor 3
    • Shinkai A, Komuta-Kunitomo M, Sato-Nakamura N, Anazawa H (2002) N-terminal domain of eotaxin-3 is important for activation of CC chemokine receptor 3. Protein Eng 15:923-929
    • (2002) Protein Eng , vol.15 , pp. 923-929
    • Shinkai, A.1    Komuta-Kunitomo, M.2    Sato-Nakamura, N.3    Anazawa, H.4
  • 91
    • 0028999259 scopus 로고    scopus 로고
    • Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type
    • Skelton NJ, Aspiras F, Ogez J, Schall TJ (2002) Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type. Biochemistry 34:5329-5342
    • (2002) Biochemistry , vol.34 , pp. 5329-5342
    • Skelton, N.J.1    Aspiras, F.2    Ogez, J.3    Schall, T.J.4
  • 92
    • 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 Fold Des 7:157-168
    • (1999) Structure Fold Des , vol.7 , pp. 157-168
    • Skelton, N.J.1    Quan, C.2    Reilly, D.3    Lowman, H.4
  • 93
    • 27144548417 scopus 로고    scopus 로고
    • Dimerization of chemokine receptors and its functional consequences
    • Springael JY, Urizar E, Parmentier M (2005) Dimerization of chemokine receptors and its functional consequences. Cytokine Growth Factor Rev 16:611-623
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 611-623
    • Springael, J.Y.1    Urizar, E.2    Parmentier, M.3
  • 94
    • 0028334630 scopus 로고
    • The N terminus of interleukin-8 (IL8) receptor confers high affinity binding to human IL8
    • Suzuki H, Prado GN, Wilkinson N, Navarro J (1994) The N terminus of interleukin-8 (IL8) receptor confers high affinity binding to human IL8. J Biol Chem 269:18263-18266
    • (1994) J Biol Chem , vol.269 , pp. 18263-18266
    • Suzuki, H.1    Prado, G.N.2    Wilkinson, N.3    Navarro, J.4
  • 99
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat Struct Biol 3:842-848
    • (1996) Nat Struct Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 100
    • 0029956647 scopus 로고    scopus 로고
    • Discrete steps in binding and signaling of interleukin-8 with its receptor
    • Wu L, Ruffing N, Shi X, Newman W, Soler D, Mackay CR, Qin S (1996) Discrete steps in binding and signaling of interleukin-8 with its receptor. J Biol Chem 271:31202-31209
    • (1996) J Biol Chem , vol.271 , pp. 31202-31209
    • Wu, L.1    Ruffing, N.2    Shi, X.3    Newman, W.4    Soler, D.5    Mackay, C.R.6    Qin, S.7
  • 101
    • 0028086420 scopus 로고
    • Structural requirements of platelet chemokines for neutrophil activation
    • Yan Z, Zhang J, Holt JC, Stewart GJ, Niewiarowski S, Poncz M (1994) Structural requirements of platelet chemokines for neutrophil activation. Blood 84:2329-2339
    • (1994) Blood , vol.84 , pp. 2329-2339
    • Yan, Z.1    Zhang, J.2    Holt, J.C.3    Stewart, G.J.4    Niewiarowski, S.5    Poncz, M.6
  • 102
    • 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
  • 103
    • 0035900771 scopus 로고    scopus 로고
    • Structural and functional characterization of human CXCR4 as a chemokine receptor and HIV-1 co-receptor by mutagenesis and molecular modeling studies
    • Zhou N, Luo Z, Luo J, Liu D, Hall JW, Pomerantz RJ, Huang Z (2001) Structural and functional characterization of human CXCR4 as a chemokine receptor and HIV-1 co-receptor by mutagenesis and molecular modeling studies. J Biol Chem 276:42826-42833
    • (2001) J Biol Chem , vol.276 , pp. 42826-42833
    • Zhou, N.1    Luo, Z.2    Luo, J.3    Liu, D.4    Hall, J.W.5    Pomerantz, R.J.6    Huang, Z.7


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