메뉴 건너뛰기




Volumn 352, Issue 5, 2005, Pages 1019-1028

crystal structure of viral macrophage inflammatory protein I encoded by Kaposi's sarcoma-associated herpesvirus at 1.7 Å

Author keywords

Chemokine; Chemotaxis; Herpesvirus; HIV

Indexed keywords

CHEMOKINE RECEPTOR CCR8; MACROPHAGE INFLAMMATORY PROTEIN 1;

EID: 24944513096     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.011     Document Type: Article
Times cited : (8)

References (71)
  • 1
    • 0842324615 scopus 로고    scopus 로고
    • Chemokines: Multiple levels of leukocyte migration control
    • B. Moser, M. Wolf, A. Walz, and P. Loetscher Chemokines: multiple levels of leukocyte migration control Trends Immunol. 25 2004 75 84
    • (2004) Trends Immunol. , vol.25 , pp. 75-84
    • Moser, B.1    Wolf, M.2    Walz, A.3    Loetscher, P.4
  • 2
    • 0035169509 scopus 로고    scopus 로고
    • The chemokine receptor CCR8 mediates human endothelial cell chemotaxis induced by I-309 and Kaposi sarcoma herpesvirus-encoded vMIP-I and by lipoprotein(a)-stimulated endothelial cell conditioned medium
    • N.S. Haque, J.T. Fallon, M.B. Taubman, and P.C. Harpel The chemokine receptor CCR8 mediates human endothelial cell chemotaxis induced by I-309 and Kaposi sarcoma herpesvirus-encoded vMIP-I and by lipoprotein(a)-stimulated endothelial cell conditioned medium Blood 97 2001 39 45
    • (2001) Blood , vol.97 , pp. 39-45
    • Haque, N.S.1    Fallon, J.T.2    Taubman, M.B.3    Harpel, P.C.4
  • 3
    • 0041835842 scopus 로고    scopus 로고
    • Monocyte chemoattractant protein-1 increases microglial infiltration and aggressiveness of gliomas
    • M. Platten, A. Kretz, U. Naumann, S. Aulwurm, K. Egashira, S. Isenmann, and M. Weller Monocyte chemoattractant protein-1 increases microglial infiltration and aggressiveness of gliomas Ann. Neurol. 54 2003 388 392
    • (2003) Ann. Neurol. , vol.54 , pp. 388-392
    • Platten, M.1    Kretz, A.2    Naumann, U.3    Aulwurm, S.4    Egashira, K.5    Isenmann, S.6    Weller, M.7
  • 4
    • 0344688307 scopus 로고    scopus 로고
    • The stromal cell-derived factor-1α/CXCR4 ligand-receptor axis is critical for progenitor survival and migration in the pancreas
    • A.G. Kayali, K. Van Gunst, I.L. Campbell, A. Stotland, M. Kritzik, and G. Liu The stromal cell-derived factor-1α/CXCR4 ligand-receptor axis is critical for progenitor survival and migration in the pancreas J. Cell. Biol. 163 2003 859 869
    • (2003) J. Cell. Biol. , vol.163 , pp. 859-869
    • Kayali, A.G.1    Van Gunst, K.2    Campbell, I.L.3    Stotland, A.4    Kritzik, M.5    Liu, G.6
  • 5
    • 0029837991 scopus 로고    scopus 로고
    • Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV
    • P.S. Moore, C. Boshoff, R.A. Weiss, and Y. Chang Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV Science 274 1996 1739 1744
    • (1996) Science , vol.274 , pp. 1739-1744
    • Moore, P.S.1    Boshoff, C.2    Weiss, R.A.3    Chang, Y.4
  • 6
    • 0035991694 scopus 로고    scopus 로고
    • Kaposi's sarcoma biology
    • C. Boshoff Kaposi's sarcoma biology IUBMB Life 53 2002 259 261
    • (2002) IUBMB Life , vol.53 , pp. 259-261
    • Boshoff, C.1
  • 7
    • 0037320390 scopus 로고    scopus 로고
    • Insights into the molecular biology and sero-epidemiology of Kaposi's sarcoma
    • J. Stebbing, S. Portsmouth, and M. Bower Insights into the molecular biology and sero-epidemiology of Kaposi's sarcoma Curr. Opin. Infect. Dis. 16 2003 25 31
    • (2003) Curr. Opin. Infect. Dis. , vol.16 , pp. 25-31
    • Stebbing, J.1    Portsmouth, S.2    Bower, M.3
  • 8
    • 0036275066 scopus 로고    scopus 로고
    • Update on Kaposi's sarcoma and other HHV8 associated diseases. Part 2: Pathogenesis, Castleman's disease, and pleural effusion lymphoma
    • U.R. Hengge, T. Ruzicka, S.K. Tyring, M. Stuschke, M. Roggendorf, R.A. Schwartz, and S. Seeber Update on Kaposi's sarcoma and other HHV8 associated diseases. Part 2: pathogenesis, Castleman's disease, and pleural effusion lymphoma Lancet Infect. Dis. 2 2002 344 352
    • (2002) Lancet Infect. Dis. , vol.2 , pp. 344-352
    • Hengge, U.R.1    Ruzicka, T.2    Tyring, S.K.3    Stuschke, M.4    Roggendorf, M.5    Schwartz, R.A.6    Seeber, S.7
  • 10
    • 0033591634 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-related herpesvirus (KSHV)-encoded chemokine vMIP-I is a specific agonist for the CC chemokine receptor (CCR)8
    • M.J. Endres, C.G. Garlisi, H. Xiao, L. Shan, and J.A. Hedrick The Kaposi's sarcoma-related herpesvirus (KSHV)-encoded chemokine vMIP-I is a specific agonist for the CC chemokine receptor (CCR)8 J. Expt. Med. 189 1999 1993 1998
    • (1999) J. Expt. Med. , vol.189 , pp. 1993-1998
    • Endres, M.J.1    Garlisi, C.G.2    Xiao, H.3    Shan, L.4    Hedrick, J.A.5
  • 11
    • 0038732559 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (KSHV)-encoded vMIP-I and vMIP-II induce signal transduction and chemotaxis in monocytic cells
    • K. Nakano, Y. Isegawa, P. Zou, K. Tadagaki, R. Inagi, and K. Yamanishi Kaposi's sarcoma-associated herpesvirus (KSHV)-encoded vMIP-I and vMIP-II induce signal transduction and chemotaxis in monocytic cells Arch. Virol. 148 2003 871 890
    • (2003) Arch. Virol. , vol.148 , pp. 871-890
    • Nakano, K.1    Isegawa, Y.2    Zou, P.3    Tadagaki, K.4    Inagi, R.5    Yamanishi, K.6
  • 12
    • 0033618444 scopus 로고    scopus 로고
    • HHV8-encoded vMIP-I selectively engages chemokine receptor CCR8. Agonist and antagonist profiles of viral chemokines
    • D.J. Dairaghi, R.A. Fan, B.E. McMaster, M.R. Hanley, and T.J. Schall HHV8-encoded vMIP-I selectively engages chemokine receptor CCR8. Agonist and antagonist profiles of viral chemokines J. Biol. Chem. 274 1999 21569 21574
    • (1999) J. Biol. Chem. , vol.274 , pp. 21569-21574
    • Dairaghi, D.J.1    Fan, R.A.2    McMaster, B.E.3    Hanley, M.R.4    Schall, T.J.5
  • 14
    • 0035903307 scopus 로고    scopus 로고
    • Unique chemotactic response profile and specific expression of chemokine receptors CCR4 and CCR8 by CD4(+)CD25(+) regulatory T cells
    • A. Iellem, M. Mariani, R. Lang, H. Recalde, P. Panina-Bordignon, F. Sinigaglia, and D. D'Ambrosio Unique chemotactic response profile and specific expression of chemokine receptors CCR4 and CCR8 by CD4(+)CD25(+) regulatory T cells J. Expt. Med. 194 2001 847 853
    • (2001) J. Expt. Med. , vol.194 , pp. 847-853
    • Iellem, A.1    Mariani, M.2    Lang, R.3    Recalde, H.4    Panina-Bordignon, P.5    Sinigaglia, F.6    D'Ambrosio, D.7
  • 16
    • 0024555819 scopus 로고
    • The three-dimensional structure of bovine platelet factor 4 at 3.0 Å resolution
    • R. St Charles, D.A. Walz, and B.F. Edwards The three-dimensional structure of bovine platelet factor 4 at 3.0 Å resolution J. Biol. Chem. 264 1989 2092 2099
    • (1989) J. Biol. Chem. , vol.264 , pp. 2092-2099
    • St Charles, R.1    Walz, D.A.2    Edwards, B.F.3
  • 17
    • 0346667110 scopus 로고    scopus 로고
    • Structure-function relationship between the human chemokine receptor CXCR3 and its ligands
    • I. Clark-Lewis, I. Mattioli, J.H. Gong, and P. Loetscher Structure-function relationship between the human chemokine receptor CXCR3 and its ligands J. Biol. Chem. 278 2003 289 295
    • (2003) J. Biol. Chem. , vol.278 , pp. 289-295
    • Clark-Lewis, I.1    Mattioli, I.2    Gong, J.H.3    Loetscher, P.4
  • 18
    • 0029670775 scopus 로고    scopus 로고
    • Deletion of the NH2-terminal residue converts monocyte chemotactic protein 1 from an activator of basophil mediator release to an eosinophil chemoattractant
    • M. Weber, M. Uguccioni, M. Baggiolini, I. Clark-Lewis, and C.A. Dahinden Deletion of the NH2-terminal residue converts monocyte chemotactic protein 1 from an activator of basophil mediator release to an eosinophil chemoattractant J. Expt. Med. 183 1996 681 685
    • (1996) J. Expt. Med. , vol.183 , pp. 681-685
    • Weber, M.1    Uguccioni, M.2    Baggiolini, M.3    Clark-Lewis, I.4    Dahinden, C.A.5
  • 20
    • 0034710999 scopus 로고    scopus 로고
    • Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation
    • E.J. Fernandez, J. Wilken, D.A. Thompson, S.C. Peiper, and E. Lolis Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation Biochemistry 39 2000 12837 12844
    • (2000) Biochemistry , vol.39 , pp. 12837-12844
    • Fernandez, E.J.1    Wilken, J.2    Thompson, D.A.3    Peiper, S.C.4    Lolis, E.5
  • 21
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF-a program to identify and analyze structural motifs in proteins
    • E.G. Hutchinson, and J.M. Thornton PROMOTIF-a program to identify and analyze structural motifs in proteins Protein Sci. 5 1996 212 220
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 23
    • 2442494318 scopus 로고    scopus 로고
    • Analysis of post-translational CCR8 modifications and their influence on receptor activity
    • J. Gutierrez, L. Kremer, A. Zaballos, I. Goya, A.C. Martinez, and G. Marquez Analysis of post-translational CCR8 modifications and their influence on receptor activity J. Biol. Chem. 279 2004 14726 14733
    • (2004) J. Biol. Chem. , vol.279 , pp. 14726-14733
    • Gutierrez, J.1    Kremer, L.2    Zaballos, A.3    Goya, I.4    Martinez, A.C.5    Marquez, G.6
  • 24
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • I.K. McDonald, and J.M. Thornton Satisfying hydrogen bonding potential in proteins J. Mol. Biol. 238 1994 777 793
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 25
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution
    • S. Sheriff, W.A. Hendrickson, and J.L. Smith Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution J. Mol. Biol. 197 1987 273 296
    • (1987) J. Mol. Biol. , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3
  • 27
    • 0037020263 scopus 로고    scopus 로고
    • The structure of human macrophage inflammatory protein-3α /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human β-defensins
    • D.M. Hoover, C. Boulegue, D. Yang, J.J. Oppenheim, K. Tucker, W. Lu, and J. Lubkowski The structure of human macrophage inflammatory protein-3α /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human β-defensins J. Biol. Chem. 277 2002 37647 37654
    • (2002) J. Biol. Chem. , vol.277 , pp. 37647-37654
    • Hoover, D.M.1    Boulegue, C.2    Yang, D.3    Oppenheim, J.J.4    Tucker, K.5    Lu, W.6    Lubkowski, J.7
  • 28
    • 0032499624 scopus 로고    scopus 로고
    • Solution structure of murine macrophage inflammatory protein-2
    • W. Shao, L.F. Jerva, J. West, E. Lolis, and B.I. Schweitzer Solution structure of murine macrophage inflammatory protein-2 Biochemistry 37 1998 8303 8313
    • (1998) Biochemistry , vol.37 , pp. 8303-8313
    • Shao, W.1    Jerva, L.F.2    West, J.3    Lolis, E.4    Schweitzer, B.I.5
  • 32
    • 0032782574 scopus 로고    scopus 로고
    • Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES
    • J. Wilken, D. Hoover, D.A. Thompson, P.N. Barlow, H. McSparron, and L. Picard Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES Chem. Biol. 6 1999 43 51
    • (1999) Chem. Biol. , vol.6 , pp. 43-51
    • Wilken, J.1    Hoover, D.2    Thompson, D.A.3    Barlow, P.N.4    McSparron, H.5    Picard, L.6
  • 34
    • 0028999259 scopus 로고
    • Proton NMR assignments and solution conformation of RANTES, a chemokine of the CC type
    • N.J. Skelton, F. Aspiras, J. Ogez, and T.J. Schall Proton NMR assignments and solution conformation of RANTES, a chemokine of the CC type Biochemistry 34 1995 5329 5342
    • (1995) Biochemistry , vol.34 , pp. 5329-5342
    • Skelton, N.J.1    Aspiras, F.2    Ogez, J.3    Schall, T.J.4
  • 35
    • 0028324332 scopus 로고
    • High-resolution solution structure of the beta chemokine hMIP-1β by multidimensional NMR
    • P.J. Lodi, D.S. Garrett, J. Kuszewski, M.L. Tsang, J.A. Weatherbee, and W.J. Leonard High-resolution solution structure of the beta chemokine hMIP-1β by multidimensional NMR Science 263 1994 1762 1767
    • (1994) Science , vol.263 , pp. 1762-1767
    • Lodi, P.J.1    Garrett, D.S.2    Kuszewski, J.3    Tsang, M.L.4    Weatherbee, J.A.5    Leonard, W.J.6
  • 38
    • 0031026207 scopus 로고    scopus 로고
    • The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions
    • J. Lubkowski, G. Bujacz, L. Boque, P.J. Domaille, T.M. Handel, and A. Wlodawer The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions Nature Struct. Biol. 4 1997 64 69
    • (1997) Nature Struct. Biol. , vol.4 , pp. 64-69
    • Lubkowski, J.1    Bujacz, G.2    Boque, L.3    Domaille, P.J.4    Handel, T.M.5    Wlodawer, A.6
  • 39
    • 0029665212 scopus 로고    scopus 로고
    • Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer
    • T.M. Handel, and P.J. Domaille Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer Biochemistry 35 1996 6569 6584
    • (1996) Biochemistry , vol.35 , pp. 6569-6584
    • Handel, T.M.1    Domaille, P.J.2
  • 40
    • 0034700312 scopus 로고    scopus 로고
    • Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors
    • J. Blaszczyk, E.V. Coillie, P. Proost, J.V. Damme, G. Opdenakker, and G.D. Bujacz Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors Biochemistry 39 2000 14075 14081
    • (2000) Biochemistry , vol.39 , pp. 14075-14081
    • Blaszczyk, J.1    Coillie, E.V.2    Proost, P.3    Damme, J.V.4    Opdenakker, G.5    Bujacz, G.D.6
  • 42
    • 0032499791 scopus 로고    scopus 로고
    • Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1α, a potent ligand for the HIV-1 "fusin" coreceptor
    • C. Dealwis, E.J. Fernandez, D.A. Thompson, R.J. Simon, M.A. Siani, and E. Lolis Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1α, a potent ligand for the HIV-1 "fusin" coreceptor Proc. Natl Acad. Sci. USA 95 1998 6941 6946
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6941-6946
    • Dealwis, C.1    Fernandez, E.J.2    Thompson, D.A.3    Simon, R.J.4    Siani, M.A.5    Lolis, E.6
  • 43
    • 0037143532 scopus 로고    scopus 로고
    • The CXCR3 binding chemokine IP-10/CXCL10: Structure and receptor interactions
    • V. Booth, D.W. Keizer, M.B. Kamphuis, I. Clark-Lewis, and B.D. Sykes The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions Biochemistry 41 2002 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
  • 44
    • 0030683638 scopus 로고    scopus 로고
    • Solution structure and basis for functional activity of stromal cell-derived factor-1; Dissociation of CXCR4 activation from binding and inhibition of HIV-1
    • M.P. Crump, J.H. Gong, P. Loetscher, K. Rajarathnam, A. Amara, and F. Arenzana-Seisdedos Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1 EMBO J. 16 1997 6996 7007
    • (1997) EMBO J. , vol.16 , pp. 6996-7007
    • Crump, M.P.1    Gong, J.H.2    Loetscher, P.3    Rajarathnam, K.4    Amara, A.5    Arenzana-Seisdedos, F.6
  • 45
    • 0028965079 scopus 로고
    • The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-Å resolution
    • M.G. Malkowski, J.Y. Wu, J.B. Lazar, P.H. Johnson, and B.F. Edwards The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-Å resolution J. Biol. Chem. 270 1995 7077 7087
    • (1995) J. Biol. Chem. , vol.270 , pp. 7077-7087
    • Malkowski, M.G.1    Wu, J.Y.2    Lazar, J.B.3    Johnson, P.H.4    Edwards, B.F.5
  • 46
    • 0034725586 scopus 로고    scopus 로고
    • The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement
    • D.M. Hoover, L.S. Mizoue, T.M. Handel, and J. Lubkowski The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement J. Biol. Chem. 275 2000 23187 23193
    • (2000) J. Biol. Chem. , vol.275 , pp. 23187-23193
    • Hoover, D.M.1    Mizoue, L.S.2    Handel, T.M.3    Lubkowski, J.4
  • 47
    • 0034724373 scopus 로고    scopus 로고
    • CC chemokine MIP-1β can function as a monomer and depends on Phe13 for receptor binding
    • J.S. Laurence, C. Blanpain, J.W. Burgner, M. Parmentier, and P.J. LiWang CC chemokine MIP-1β can function as a monomer and depends on Phe13 for receptor binding Biochemistry 39 2000 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
  • 48
    • 0030811908 scopus 로고    scopus 로고
    • Distinct but overlapping epitopes for the interaction of a CC-chemokine with CCR1, CCR3 and CCR5
    • D.R. Pakianathan, E.G. Kuta, D.R. Artis, N.J. Skelton, and C.A. Hebert Distinct but overlapping epitopes for the interaction of a CC-chemokine with CCR1, CCR3 and CCR5 Biochemistry 36 1997 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
  • 49
    • 0033522887 scopus 로고    scopus 로고
    • Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1α, MIP-1β, and RANTES. Characterization of active disaggregated chemokine variants
    • L.G. Czaplewski, J. McKeating, C.J. Craven, L.D. Higgins, V. Appay, and A. Brown Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1α, MIP-1β, and RANTES. Characterization of active disaggregated chemokine variants J. Biol. Chem. 274 1999 16077 16084
    • (1999) J. Biol. Chem. , vol.274 , pp. 16077-16084
    • Czaplewski, L.G.1    McKeating, J.2    Craven, C.J.3    Higgins, L.D.4    Appay, V.5    Brown, A.6
  • 50
  • 51
    • 1542376200 scopus 로고    scopus 로고
    • A structural and dynamic model for the interaction of interleukin-8 and glycosaminoglycans: Support from isothermal fluorescence titrations
    • E. Krieger, E. Geretti, B. Brandner, B. Goger, T.N. Wells, and A.J. Kungl A structural and dynamic model for the interaction of interleukin-8 and glycosaminoglycans: support from isothermal fluorescence titrations Proteins: Struct. Funct. Genet. 54 2004 768 775
    • (2004) Proteins: Struct. Funct. Genet. , vol.54 , pp. 768-775
    • Krieger, E.1    Geretti, E.2    Brandner, B.3    Goger, B.4    Wells, T.N.5    Kungl, A.J.6
  • 52
    • 2542498611 scopus 로고    scopus 로고
    • Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: Implications for structure and function in vivo
    • E.K. Lau, C.D. Paavola, Z. Johnson, J.P. Gaudry, E. Geretti, and F. Borlat Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo J. Biol. Chem. 279 2004 22294 22305
    • (2004) J. Biol. Chem. , vol.279 , pp. 22294-22305
    • Lau, E.K.1    Paavola, C.D.2    Johnson, Z.3    Gaudry, J.P.4    Geretti, E.5    Borlat, F.6
  • 53
    • 0037452728 scopus 로고    scopus 로고
    • Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines
    • A.E. Proudfoot, T.M. Handel, Z. Johnson, E.K. Lau, P. LiWang, and I. Clark-Lewis Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines Proc. Natl Acad. Sci. USA 100 2003 1885 1890
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1885-1890
    • Proudfoot, A.E.1    Handel, T.M.2    Johnson, Z.3    Lau, E.K.4    Liwang, P.5    Clark-Lewis, I.6
  • 54
    • 0035281612 scopus 로고    scopus 로고
    • Aggregation-independent modulation of proteoglycan binding by neutralization of C-terminal acidic residues in the chemokine macrophage inflammatory protein 1α
    • K. Ottersbach, and G.J. Graham Aggregation-independent modulation of proteoglycan binding by neutralization of C-terminal acidic residues in the chemokine macrophage inflammatory protein 1α Biochem. J. 354 2001 447 453
    • (2001) Biochem. J. , vol.354 , pp. 447-453
    • Ottersbach, K.1    Graham, G.J.2
  • 55
    • 0038608022 scopus 로고    scopus 로고
    • CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10)
    • G.S. Campanella, E.M. Lee, J. Sun, and A.D. Luster CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10) J. Biol. Chem. 278 2003 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
  • 56
    • 0033566956 scopus 로고    scopus 로고
    • Structure and function of the glycosaminoglycan binding site of chemokine macrophage-inflammatory protein-1β
    • W. Koopmann, C. Ediriwickrema, and M.S. Krangel Structure and function of the glycosaminoglycan binding site of chemokine macrophage-inflammatory protein-1β J. Immunol. 163 1999 2120 2127
    • (1999) J. Immunol. , vol.163 , pp. 2120-2127
    • Koopmann, W.1    Ediriwickrema, C.2    Krangel, M.S.3
  • 57
    • 1842477451 scopus 로고    scopus 로고
    • Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin
    • F.C. Peterson, E.S. Elgin, T.J. Nelson, F. Zhang, T.J. Hoeger, R.J. Linhardt, and B.F. Volkman Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin J. Biol. Chem. 279 2004 12598 12604
    • (2004) J. Biol. Chem. , vol.279 , pp. 12598-12604
    • Peterson, F.C.1    Elgin, E.S.2    Nelson, T.J.3    Zhang, F.4    Hoeger, T.J.5    Linhardt, R.J.6    Volkman, B.F.7
  • 58
    • 0034697016 scopus 로고    scopus 로고
    • Examination of the function of RANTES, MIP-1α, and MIP-1β following interaction with heparin-like glycosaminoglycans
    • S. Ali, A.C. Palmer, B. Banerjee, S.J. Fritchley, and J.A. Kirby Examination of the function of RANTES, MIP-1α, and MIP-1β following interaction with heparin-like glycosaminoglycans J. Biol. Chem. 275 2000 11721 11727
    • (2000) J. Biol. Chem. , vol.275 , pp. 11721-11727
    • Ali, S.1    Palmer, A.C.2    Banerjee, B.3    Fritchley, S.J.4    Kirby, J.A.5
  • 59
  • 60
    • 5644247983 scopus 로고    scopus 로고
    • Prevention of vaginal SHIV transmission in rhesus macaques through inhibition of CCR5
    • M.M. Lederman, R.S. Veazey, R. Offord, D.E. Mosier, J. Dufour, and M. Mefford Prevention of vaginal SHIV transmission in rhesus macaques through inhibition of CCR5 Science 306 2004 485 487
    • (2004) Science , vol.306 , pp. 485-487
    • Lederman, M.M.1    Veazey, R.S.2    Offord, R.3    Mosier, D.E.4    Dufour, J.5    Mefford, M.6
  • 62
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 63
    • 0028057108 scopus 로고
    • Raster3D version 2.0-a program for photorealistic molecular graphics
    • E.A. Merritt, and M.E. Murphy Raster3D version 2.0-a program for photorealistic molecular graphics Acta Crystallog. sect. A 50 1994 869 873
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 64
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct. Funct. Genet. 11 1991 281 296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 65
    • 0029831680 scopus 로고    scopus 로고
    • An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally-related subfamilies
    • L.A. Kelley, S.P. Gardner, and M.J. Sutcliffe An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally-related subfamilies Protein Eng. 9 1996 1063 1065
    • (1996) Protein Eng. , vol.9 , pp. 1063-1065
    • Kelley, L.A.1    Gardner, S.P.2    Sutcliffe, M.J.3
  • 66
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 67
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 68
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 70
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 71
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 283 291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.