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Volumn 8, Issue 9, 2013, Pages 1955-1963

Sulfopeptide probes of the CXCR4/CXCL12 interface reveal oligomer-specific contacts and chemokine allostery

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOKINE; CHEMOKINE RECEPTOR CXCR4; DIMER; MONOMER; OLIGOMER; STROMAL CELL DERIVED FACTOR 1; SULFOPEPTIDE; TYROSINE; UNCLASSIFIED DRUG;

EID: 84884609886     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb400274z     Document Type: Article
Times cited : (49)

References (52)
  • 2
    • 0032507962 scopus 로고    scopus 로고
    • Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development
    • Zou, Y. R., Kottmann, A. H., Kuroda, M., Taniuchi, I., and Littman, D. R. (1998) Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development Nature 393, 595-599
    • (1998) Nature , vol.393 , pp. 595-599
    • Zou, Y.R.1    Kottmann, A.H.2    Kuroda, M.3    Taniuchi, I.4    Littman, D.R.5
  • 5
    • 34548174756 scopus 로고    scopus 로고
    • Stromal cell derived factor-1 alpha confers protection against myocardial ischemia/reperfusion injury: Role of the cardiac stromal cell derived factor-1 alpha CXCR4 axis
    • Hu, X., Dai, S., Wu, W. J., Tan, W., Zhu, X., Mu, J., Guo, Y., Bolli, R., and Rokosh, G. (2007) Stromal cell derived factor-1 alpha confers protection against myocardial ischemia/reperfusion injury: role of the cardiac stromal cell derived factor-1 alpha CXCR4 axis Circulation 116, 654-663
    • (2007) Circulation , vol.116 , pp. 654-663
    • Hu, X.1    Dai, S.2    Wu, W.J.3    Tan, W.4    Zhu, X.5    Mu, J.6    Guo, Y.7    Bolli, R.8    Rokosh, G.9
  • 7
    • 35148816977 scopus 로고    scopus 로고
    • Antagonism of stromal cell-derived factor-1alpha reduces infarct size and improves ventricular function after myocardial infarction
    • Proulx, C., El-Helou, V., Gosselin, H., Clement, R., Gillis, M. A., Villeneuve, L., and Calderone, A. (2007) Antagonism of stromal cell-derived factor-1alpha reduces infarct size and improves ventricular function after myocardial infarction Pfluegers Arch. 455, 241-250
    • (2007) Pfluegers Arch. , vol.455 , pp. 241-250
    • Proulx, C.1    El-Helou, V.2    Gosselin, H.3    Clement, R.4    Gillis, M.A.5    Villeneuve, L.6    Calderone, A.7
  • 9
    • 3042822267 scopus 로고    scopus 로고
    • Cancer and the chemokine network
    • Balkwill, F. (2004) Cancer and the chemokine network Nat. Rev. Cancer 4, 540-550
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 540-550
    • Balkwill, F.1
  • 12
    • 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, G. J., Vasilieva, N., Wright, P. L., Kiprilov, E., Mirzabekov, T., and 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
  • 15
    • 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, A. A., Dragan, S., Kawano, T., Gavrilin, M. A., Gulina, I. V., Chakravarty, L., and Kolattukudy, P. E. (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
  • 16
    • 0035803466 scopus 로고    scopus 로고
    • Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines
    • Bannert, N., Craig, S., Farzan, M., Sogah, D., Santo, N. V., Choe, H., and Sodroski, J. (2001) Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines J. Exp. Med. 194, 1661-1673
    • (2001) J. Exp. Med. , vol.194 , pp. 1661-1673
    • Bannert, N.1    Craig, S.2    Farzan, M.3    Sogah, D.4    Santo, N.V.5    Choe, H.6    Sodroski, J.7
  • 17
    • 33746505443 scopus 로고    scopus 로고
    • CXCR3 requires tyrosine sulfation for ligand binding and a second extracellular loop arginine residue for ligand-induced chemotaxis
    • Colvin, R. A., Campanella, G. S., Manice, L. A., and Luster, A. D. (2006) CXCR3 requires tyrosine sulfation for ligand binding and a second extracellular loop arginine residue for ligand-induced chemotaxis Mol. Cell. Biol. 26, 5838-5849
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5838-5849
    • Colvin, R.A.1    Campanella, G.S.2    Manice, L.A.3    Luster, A.D.4
  • 18
    • 2442494318 scopus 로고    scopus 로고
    • Analysis of post-translational CCR8 modifications and their influence on receptor activity
    • Gutierrez, J., Kremer, L., Zaballos, A., Goya, I., Martinez, A. C., and Marquez, G. (2004) Analysis of post-translational CCR8 modifications and their influence on receptor activity J. Biol. Chem. 279, 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
  • 19
    • 0037204744 scopus 로고    scopus 로고
    • CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion
    • Fong, A. M., Alam, S. M., Imai, T., Haribabu, B., and Patel, D. D. (2002) CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion J. Biol. Chem. 277, 19418-19423
    • (2002) J. Biol. Chem. , vol.277 , pp. 19418-19423
    • Fong, A.M.1    Alam, S.M.2    Imai, T.3    Haribabu, B.4    Patel, D.D.5
  • 22
    • 0034724373 scopus 로고    scopus 로고
    • CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding
    • Laurence, J. S., Blanpain, C., Burgner, J. W., Parmentier, M., and LiWang, P. J. (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
  • 27
    • 84869226562 scopus 로고    scopus 로고
    • A locked, dimeric CXCL12 variant effectively inhibits pulmonary metastasis of CXCR4-expressing melanoma cells due to enhanced serum stability
    • Takekoshi, T., Ziarek, J. J., Volkman, B. F., and Hwang, S. T. (2012) A locked, dimeric CXCL12 variant effectively inhibits pulmonary metastasis of CXCR4-expressing melanoma cells due to enhanced serum stability Mol. Cancer Ther. 11, 2516-2525
    • (2012) Mol. Cancer Ther. , vol.11 , pp. 2516-2525
    • Takekoshi, T.1    Ziarek, J.J.2    Volkman, B.F.3    Hwang, S.T.4
  • 28
    • 33745173829 scopus 로고    scopus 로고
    • Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1alpha (SDF-1alpha/CXCL12)
    • Veldkamp, C. T., Seibert, C., Peterson, F. C., Sakmar, T. P., and Volkman, B. F. (2006) Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1alpha (SDF-1alpha/CXCL12) J. Mol. Biol. 359, 1400-1409
    • (2006) J. Mol. Biol. , vol.359 , pp. 1400-1409
    • Veldkamp, C.T.1    Seibert, C.2    Peterson, F.C.3    Sakmar, T.P.4    Volkman, B.F.5
  • 29
    • 77952813636 scopus 로고    scopus 로고
    • Targeting SDF-1/CXCL12 with a ligand that prevents activation of CXCR4 through structure-based drug design
    • Veldkamp, C. T., Ziarek, J. J., Peterson, F. C., Chen, Y., and Volkman, B. F. (2010) Targeting SDF-1/CXCL12 with a ligand that prevents activation of CXCR4 through structure-based drug design J. Am. Chem. Soc. 132, 7242-7243
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7242-7243
    • Veldkamp, C.T.1    Ziarek, J.J.2    Peterson, F.C.3    Chen, Y.4    Volkman, B.F.5
  • 31
    • 79959708032 scopus 로고    scopus 로고
    • Sulfotyrosine recognition as marker for druggable sites in the extracellular space
    • Ziarek, J. J., Heroux, M. S., Veldkamp, C. T., Peterson, F. C., and Volkman, B. F. (2011) Sulfotyrosine recognition as marker for druggable sites in the extracellular space Int. J. Mol. Sci. 12, 3740-3756
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 3740-3756
    • Ziarek, J.J.1    Heroux, M.S.2    Veldkamp, C.T.3    Peterson, F.C.4    Volkman, B.F.5
  • 32
    • 15244345079 scopus 로고    scopus 로고
    • The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin
    • Veldkamp, C. T., Peterson, F. C., Pelzek, A. J., and Volkman, B. F. (2005) The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin Protein Sci. 14, 1071-1081
    • (2005) Protein Sci. , vol.14 , pp. 1071-1081
    • Veldkamp, C.T.1    Peterson, F.C.2    Pelzek, A.J.3    Volkman, B.F.4
  • 34
    • 0141506109 scopus 로고    scopus 로고
    • Disulfide by Design: A computational method for the rational design of disulfide bonds in proteins
    • Dombkowski, A. A. (2003) Disulfide by Design: a computational method for the rational design of disulfide bonds in proteins Bioinformatics 19, 1852-1853
    • (2003) Bioinformatics , vol.19 , pp. 1852-1853
    • Dombkowski, A.A.1
  • 35
    • 10044240717 scopus 로고    scopus 로고
    • Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha
    • Gozansky, E. K., Louis, J. M., Caffrey, M., and Clore, G. M. (2005) Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha J. Mol. Biol. 345, 651-658
    • (2005) J. Mol. Biol. , vol.345 , pp. 651-658
    • Gozansky, E.K.1    Louis, J.M.2    Caffrey, M.3    Clore, G.M.4
  • 36
    • 60549105011 scopus 로고    scopus 로고
    • Regulation of chemokine recognition by site-specific tyrosine sulfation of receptor peptides
    • Simpson, L. S., Zhu, J. Z., Widlanski, T. S., and Stone, M. J. (2009) Regulation of chemokine recognition by site-specific tyrosine sulfation of receptor peptides Chem. Biol. 16, 153-161
    • (2009) Chem. Biol. , vol.16 , pp. 153-161
    • Simpson, L.S.1    Zhu, J.Z.2    Widlanski, T.S.3    Stone, M.J.4
  • 37
  • 38
    • 84875988747 scopus 로고    scopus 로고
    • Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1)
    • Tan, J. H., Ludeman, J. P., Wedderburn, J., Canals, M., Hall, P., Butler, S. J., Taleski, D., Christopoulos, A., Hickey, M. J., Payne, R. J., and Stone, M. J. (2013) Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1) J. Biol. Chem. 288, 10024-10034
    • (2013) J. Biol. Chem. , vol.288 , pp. 10024-10034
    • Tan, J.H.1    Ludeman, J.P.2    Wedderburn, J.3    Canals, M.4    Hall, P.5    Butler, S.J.6    Taleski, D.7    Christopoulos, A.8    Hickey, M.J.9    Payne, R.J.10    Stone, M.J.11
  • 39
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J. A. and McClendon, C. L. (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature 450, 1001-1009
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 40
    • 84865560861 scopus 로고    scopus 로고
    • Characterization of tyrosine sulphation in rFVIII (turoctocog alfa) expressed in CHO and HEK-293 cells
    • Nielsen, P. F., Bak, S., and Vandahl, B. (2012) Characterization of tyrosine sulphation in rFVIII (turoctocog alfa) expressed in CHO and HEK-293 cells Haemophilia 18, e397-398
    • (2012) Haemophilia , vol.18 , pp. 397-398
    • Nielsen, P.F.1    Bak, S.2    Vandahl, B.3
  • 41
    • 33845767989 scopus 로고    scopus 로고
    • Recognition of RANTES by extracellular parts of the CCR5 receptor
    • Duma, L., Haussinger, D., Rogowski, M., Lusso, P., and Grzesiek, S. (2007) Recognition of RANTES by extracellular parts of the CCR5 receptor J. Mol. Biol. 365, 1063-1075
    • (2007) J. Mol. Biol. , vol.365 , pp. 1063-1075
    • Duma, L.1    Haussinger, D.2    Rogowski, M.3    Lusso, P.4    Grzesiek, S.5
  • 42
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T. and Nash, P. (2003) Assembly of cell regulatory systems through protein interaction domains Science 300, 445-452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 43
    • 41149120313 scopus 로고    scopus 로고
    • SLiMFinder: A probabilistic method for identifying over-represented, convergently evolved, short linear motifs in proteins
    • Edwards, R. J., Davey, N. E., and Shields, D. C. (2007) SLiMFinder: a probabilistic method for identifying over-represented, convergently evolved, short linear motifs in proteins PLoS One 2, e967
    • (2007) PLoS One , vol.2 , pp. 967
    • Edwards, R.J.1    Davey, N.E.2    Shields, D.C.3
  • 44
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: Versatile signaling module and pharmaceutical target
    • Machida, K. and Mayer, B. J. (2005) The SH2 domain: versatile signaling module and pharmaceutical target Biochim. Biophys. Acta 1747, 1-25
    • (2005) Biochim. Biophys. Acta , vol.1747 , pp. 1-25
    • Machida, K.1    Mayer, B.J.2
  • 45
    • 84866338076 scopus 로고    scopus 로고
    • Druggability analysis and structural classification of bromodomain acetyl-lysine binding sites
    • Vidler, L. R., Brown, N., Knapp, S., and Hoelder, S. (2012) Druggability analysis and structural classification of bromodomain acetyl-lysine binding sites J. Med. Chem. 55, 7346-7359
    • (2012) J. Med. Chem. , vol.55 , pp. 7346-7359
    • Vidler, L.R.1    Brown, N.2    Knapp, S.3    Hoelder, S.4
  • 46
    • 80455131079 scopus 로고    scopus 로고
    • Drug discovery toward antagonists of methyl-lysine binding proteins
    • Herold, J. M., Ingerman, L. A., Gao, C., and Frye, S. V. (2011) Drug discovery toward antagonists of methyl-lysine binding proteins Curr. Chem. Genomics 5, 51-61
    • (2011) Curr. Chem. Genomics , vol.5 , pp. 51-61
    • Herold, J.M.1    Ingerman, L.A.2    Gao, C.3    Frye, S.V.4
  • 47
    • 67349111690 scopus 로고    scopus 로고
    • Tyrosine sulfation: An increasingly recognised post-translational modification of secreted proteins
    • Stone, M. J., Chuang, S., Hou, X., Shoham, M., and Zhu, J. Z. (2009) Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins New Biotechnol. 25, 299-317
    • (2009) New Biotechnol. , vol.25 , pp. 299-317
    • Stone, M.J.1    Chuang, S.2    Hou, X.3    Shoham, M.4    Zhu, J.Z.5
  • 48
    • 63849217132 scopus 로고    scopus 로고
    • Diversity of polyproline recognition by EVH1 domains
    • Peterson, F. C. and Volkman, B. F. (2009) Diversity of polyproline recognition by EVH1 domains Front. Biosci. 14, 833-846
    • (2009) Front. Biosci. , vol.14 , pp. 833-846
    • Peterson, F.C.1    Volkman, B.F.2
  • 49
    • 0036088377 scopus 로고    scopus 로고
    • The Sulfinator: Predicting tyrosine sulfation sites in protein sequences
    • Monigatti, F., Gasteiger, E., Bairoch, A., and Jung, E. (2002) The Sulfinator: predicting tyrosine sulfation sites in protein sequences Bioinformatics 18, 769-770
    • (2002) Bioinformatics , vol.18 , pp. 769-770
    • Monigatti, F.1    Gasteiger, E.2    Bairoch, A.3    Jung, E.4
  • 52
    • 79952366609 scopus 로고    scopus 로고
    • Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach
    • Ziarek, J. J., Peterson, F. C., Lytle, B. L., and Volkman, B. F. (2011) Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach Methods Enzymol. 493, 241-275
    • (2011) Methods Enzymol. , vol.493 , pp. 241-275
    • Ziarek, J.J.1    Peterson, F.C.2    Lytle, B.L.3    Volkman, B.F.4


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