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Volumn 62, Issue , 2015, Pages 97-104

Identification and characterization of a glycosaminoglycan binding site on interleukin-10 via molecular simulation methods

Author keywords

GAG binding; Glycosaminoglycan; Interleukin 10; Molecular dynamics; Molecular modeling

Indexed keywords

BINDING ENERGY; BINS; BIOLOGICAL SYSTEMS; COMPUTATIONAL CHEMISTRY; ELECTRIC FIELDS; HYDROGEN BONDS; IMPORTANCE SAMPLING; MOLECULAR DYNAMICS; MOLECULAR MODELING;

EID: 84942798725     PISSN: 10933263     EISSN: 18734243     Source Type: Journal    
DOI: 10.1016/j.jmgm.2015.09.003     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 0035062021 scopus 로고    scopus 로고
    • R. de Waal Malefyt, R. L. Coffman, A. O'Garra, Interleukin-10 and the interleukin-10 receptor
    • K.W. Moore R. de Waal Malefyt, R. L. Coffman, A. O'Garra, Interleukin-10 and the interleukin-10 receptor Ann. Rev. Immunol. 19 1 2001 683
    • (2001) Ann. Rev. Immunol. , vol.19 , Issue.1 , pp. 683
    • Moore, K.W.1
  • 2
    • 0024408824 scopus 로고
    • Two types of mouse T helper cell. IV. Th2 clones secrete a factor that inhibits cytokine production by Th1 clones
    • D.F. Fiorentino, M.W. Bond, and T.R. Mosmann Two types of mouse T helper cell. IV. Th2 clones secrete a factor that inhibits cytokine production by Th1 clones J. Exp. Med. 170 6 1989 2081 2095 10.1084/jem.170.6.2081
    • (1989) J. Exp. Med. , vol.170 , Issue.6 , pp. 2081-2095
    • Fiorentino, D.F.1    Bond, M.W.2    Mosmann, T.R.3
  • 4
    • 0026607155 scopus 로고
    • IL-10 inhibits mitogen-induced T cell proliferation by selectively inhibiting macrophage costimulatory function
    • L. Ding, and E.M. Shevach IL-10 inhibits mitogen-induced T cell proliferation by selectively inhibiting macrophage costimulatory function J. Immunol. 148 10 1992 3133 3139
    • (1992) J. Immunol. , vol.148 , Issue.10 , pp. 3133-3139
    • Ding, L.1    Shevach, E.M.2
  • 5
    • 0027521572 scopus 로고
    • Interleukin-10-deficient mice develop chronic enterocolitis
    • R. Kühn, J. Löhler, D. Rennick, K. Rajewsky, and W. Müller Interleukin-10-deficient mice develop chronic enterocolitis Cell 75 2 1993 263 274 10.1016/0092-8674(93)80068-P
    • (1993) Cell , vol.75 , Issue.2 , pp. 263-274
    • Kühn, R.1    Löhler, J.2    Rennick, D.3    Rajewsky, K.4    Müller, W.5
  • 7
    • 0038283161 scopus 로고    scopus 로고
    • Interleukin-10 therapy-review of a new approach
    • K. Asadullah, W. Sterry, and H.D. Volk Interleukin-10 therapy-review of a new approach Pharmacol. Rev. 55 2 2003 241 269 10.1124/pr.55.2
    • (2003) Pharmacol. Rev. , vol.55 , Issue.2 , pp. 241-269
    • Asadullah, K.1    Sterry, W.2    Volk, H.D.3
  • 8
    • 41649089306 scopus 로고    scopus 로고
    • Distinct functions of interleukin-10 derived from different cellular sources
    • A. Roers, and W. Müller Distinct functions of interleukin-10 derived from different cellular sources Curr. Immunol. Rev. 4 1 2008 37 42 10.2174/157339508783597262
    • (2008) Curr. Immunol. Rev. , vol.4 , Issue.1 , pp. 37-42
    • Roers, A.1    Müller, W.2
  • 9
    • 55149094739 scopus 로고    scopus 로고
    • Interleukin-10: New perspectives on an old cytokine
    • D.M. Mosser, and X. Zhang Interleukin-10: new perspectives on an old cytokine Immunol. Rev. 226 2008 205 218 10.1111/j.1600-065X.2008.00706.x
    • (2008) Immunol. Rev. , vol.226 , pp. 205-218
    • Mosser, D.M.1    Zhang, X.2
  • 11
    • 0034284058 scopus 로고    scopus 로고
    • Heparin and heparan sulfate bind interleukin-10 and modulate its activity
    • S. Salek-Ardakani, J.R. Arrand, D. Shaw, and M. Mackett Heparin and heparan sulfate bind interleukin-10 and modulate its activity Blood 96 2000 1879 1888
    • (2000) Blood , vol.96 , pp. 1879-1888
    • Salek-Ardakani, S.1    Arrand, J.R.2    Shaw, D.3    Mackett, M.4
  • 12
    • 84911104975 scopus 로고    scopus 로고
    • NMR characterization of the binding properties and conformation of glycosaminoglycans interacting with interleukin-10
    • G. Künze, J.-P. Gehrcke, M.T. Pisabarro, and D. Huster NMR characterization of the binding properties and conformation of glycosaminoglycans interacting with interleukin-10 Glycobiology 24 11 2014 1036 1049 10.1093/glycob/cwu069
    • (2014) Glycobiology , vol.24 , Issue.11 , pp. 1036-1049
    • Künze, G.1    Gehrcke, J.-P.2    Pisabarro, M.T.3    Huster, D.4
  • 13
    • 77953684080 scopus 로고    scopus 로고
    • Proteoglycans and sulfated glycosaminoglycans
    • E.J. Varki A, R.D. Cummings, 2nd ed. Cold Spring Harbor Laboratory Press
    • L.U. Esko, and J.D. Kimata K Proteoglycans and sulfated glycosaminoglycans E.J. Varki A, R.D. Cummings, Essentials of Glycobiology 2nd ed. 2009 Cold Spring Harbor Laboratory Press
    • (2009) Essentials of Glycobiology
    • Esko, L.U.1    Kimata, K.J.D.2
  • 14
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • L. Pellegrini, D.F. Burke, F.v. Delft, B. Mulloy, and T.L. Blundell Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin Nature 407 6807 2000 1029 1034 10.1038/35039551
    • (2000) Nature , vol.407 , Issue.6807 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Delft, F.V.3    Mulloy, B.4    Blundell, T.L.5
  • 15
    • 0033635299 scopus 로고    scopus 로고
    • Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization
    • J. Schlessinger, A.N. Plotnikov, O.A. Ibrahimi, A.V. Eliseenkova, B.K. Yeh, A. Yayon, R.J. Linhardt, and M. Mohammadi Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization Mol. Cell 6 3 2000 743 750 10.1016/S1097-2765(00)00073-3
    • (2000) Mol. Cell , vol.6 , Issue.3 , pp. 743-750
    • Schlessinger, J.1    Plotnikov, A.N.2    Ibrahimi, O.A.3    Eliseenkova, A.V.4    Yeh, B.K.5    Yayon, A.6    Linhardt, R.J.7    Mohammadi, M.8
  • 16
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - As exemplified by chemokines.
    • T.M. Handel, Z. Johnson, S.E. Crown, E.K. Lau, M. Sweeney, and A.E. Proudfoot Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Ann. Rev. Biochem. 74 1 2005 385 410 10.1146/annurev.biochem.72.121801.161747
    • (2005) Ann. Rev. Biochem. , vol.74 , Issue.1 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Sweeney, M.5    Proudfoot, A.E.6
  • 17
    • 33846548566 scopus 로고    scopus 로고
    • Structural view of glycosaminoglycan-protein interactions
    • A. Imberty, H. Lortat-Jacob, and S. Pérez Structural view of glycosaminoglycan-protein interactions Carbohydr. Res. 342 3 2007 430 439 10.1016/j.carres.2006.12.019
    • (2007) Carbohydr. Res. , vol.342 , Issue.3 , pp. 430-439
    • Imberty, A.1    Lortat-Jacob, H.2    Pérez, S.3
  • 18
    • 56649100319 scopus 로고    scopus 로고
    • The structure of glycosaminoglycans and their interactions with proteins
    • N. Gandhi, and R. Mancera The structure of glycosaminoglycans and their interactions with proteins Chem. Biol. Drug Des. 72 6 2008 455 482 10.1111/j.1747-0285.2008.00741.x
    • (2008) Chem. Biol. Drug Des. , vol.72 , Issue.6 , pp. 455-482
    • Gandhi, N.1    Mancera, R.2
  • 19
    • 84894667941 scopus 로고    scopus 로고
    • Flexibility and explicit solvent in molecular dynamics-based docking of protein-glycosaminoglycan systems
    • S.A. Samsonov, J.-P. Gehrcke, and M.T. Pisabarro Flexibility and explicit solvent in molecular dynamics-based docking of protein-glycosaminoglycan systems J. Chem. Inf. Model. 54 2 2014 582 592 10.1021/ci4006047
    • (2014) J. Chem. Inf. Model. , vol.54 , Issue.2 , pp. 582-592
    • Samsonov, S.A.1    Gehrcke, J.-P.2    Pisabarro, M.T.3
  • 20
    • 0029995691 scopus 로고    scopus 로고
    • Crystal structure of human interleukin-10 at 1.6 Å resolution and a model of a complex with its soluble receptor
    • A. Zdanov, C. Schalk-Hihi, and A. Wlodawer Crystal structure of human interleukin-10 at 1.6 Å resolution and a model of a complex with its soluble receptor Protein Science 5 10 1996 1955 1962 10.1002/pro.5560051001
    • (1996) Protein Science , vol.5 , Issue.10 , pp. 1955-1962
    • Zdanov, A.1    Schalk-Hihi, C.2    Wlodawer, A.3
  • 21
    • 0032397258 scopus 로고    scopus 로고
    • Structural and biological stability of the human interleukin 10 homodimer
    • R. Syto, N.J. Murgolo, E.H. Braswell, P. Mui, E. Huang, and W.T. Windsor Structural and biological stability of the human interleukin 10 homodimer Biochemistry 37 48 1998 16943 16951 10.1021/bi981555y
    • (1998) Biochemistry , vol.37 , Issue.48 , pp. 16943-16951
    • Syto, R.1    Murgolo, N.J.2    Braswell, E.H.3    Mui, P.4    Huang, E.5    Windsor, W.T.6
  • 22
    • 78649744210 scopus 로고    scopus 로고
    • Structural analysis of cytokines comprising the IL-10 family
    • A. Zdanov Structural analysis of cytokines comprising the IL-10 family Cytokine Growth Factor Rev. 21 5 2010 325 330
    • (2010) Cytokine Growth Factor Rev. , vol.21 , Issue.5 , pp. 325-330
    • Zdanov, A.1
  • 26
    • 84884192184 scopus 로고    scopus 로고
    • Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald
    • R. Salomon-Ferrer, A.W. Götz, D. Poole, S. Le Grand, and R.C. Walker Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald J. Chem. Theory Comput. 9 9 2013 3878 3888 10.1021/ct400314y
    • (2013) J. Chem. Theory Comput. , vol.9 , Issue.9 , pp. 3878-3888
    • Salomon-Ferrer, R.1    Götz, A.W.2    Poole, D.3    Le Grand, S.4    Walker, R.C.5
  • 28
    • 84880022273 scopus 로고    scopus 로고
    • PTRAJ and CPPTRAJ: Software for processing and analysis of molecular dynamics trajectory data
    • D.R. Roe, and T.E. Cheatham PTRAJ and CPPTRAJ: software for processing and analysis of molecular dynamics trajectory data J. Chem. Theory Comput. 9 7 2013 3084 3095 10.1021/ct400341p
    • (2013) J. Chem. Theory Comput. , vol.9 , Issue.7 , pp. 3084-3095
    • Roe, D.R.1    Cheatham, T.E.2
  • 30
    • 0029644946 scopus 로고
    • Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma
    • A. Zdanov, C. Schalk-Hihi, A. Gustchina, M. Tsang, J. Weatherbee, and A. Wlodawer Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma Structure 3 6 1995 591 601 10.1016/S0969-2126(01)00193-9
    • (1995) Structure , vol.3 , Issue.6 , pp. 591-601
    • Zdanov, A.1    Schalk-Hihi, C.2    Gustchina, A.3    Tsang, M.4    Weatherbee, J.5    Wlodawer, A.6
  • 31
    • 78649746427 scopus 로고    scopus 로고
    • IL-10 family of cytokines
    • R. Sabat IL-10 family of cytokines Cytokine Growth Factor Rev. 21 5 2010 315 324 10.1016/j.cytogfr.2010.11.001
    • (2010) Cytokine Growth Factor Rev. , vol.21 , Issue.5 , pp. 315-324
    • Sabat, R.1
  • 32
    • 0034897552 scopus 로고    scopus 로고
    • Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site
    • K. Josephson, N.J. Logsdon, and M.R. Walter Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site Immunity 15 1 2001 35 46 10.1016/S1074-7613(01)00169-8
    • (2001) Immunity , vol.15 , Issue.1 , pp. 35-46
    • Josephson, K.1    Logsdon, N.J.2    Walter, M.R.3
  • 34
    • 17044411254 scopus 로고    scopus 로고
    • Same structure, different function: Crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain
    • S.I. Yoon, B.C. Jones, N.J. Logsdon, and M.R. Walter Same structure, different function: crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain Structure 13 4 2005 551 564 doi:10.1016/j.str.2005.01.016
    • (2005) Structure , vol.13 , Issue.4 , pp. 551-564
    • Yoon, S.I.1    Jones, B.C.2    Logsdon, N.J.3    Walter, M.R.4
  • 35
    • 24044463925 scopus 로고    scopus 로고
    • A model of the ternary complex of interleukin-10 with its soluble receptors
    • S. Pletnev, E. Magracheva, A. Wlodawer, and A. Zdanov A model of the ternary complex of interleukin-10 with its soluble receptors BMC Struct. Biol. 5 1 2005 10 10.1186/1472-6807-5-10
    • (2005) BMC Struct. Biol. , vol.5 , Issue.1 , pp. 10
    • Pletnev, S.1    Magracheva, E.2    Wlodawer, A.3    Zdanov, A.4
  • 36
    • 33845948477 scopus 로고    scopus 로고
    • Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex
    • S.I. Yoon, N.J. Logsdon, F. Sheikh, R.P. Donnelly, and M.R. Walter Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex J. Biol. Chem. 281 46 2006 35088 35096 10.1074/jbc.M606791200
    • (2006) J. Biol. Chem. , vol.281 , Issue.46 , pp. 35088-35096
    • Yoon, S.I.1    Logsdon, N.J.2    Sheikh, F.3    Donnelly, R.P.4    Walter, M.R.5
  • 37
    • 84864498078 scopus 로고    scopus 로고
    • Structural basis for receptor sharing and activation by interleukin-20 receptor-2 (IL-20R2) binding cytokines
    • N.J. Logsdon, A. Deshpande, B.D. Harris, K.R. Rajashankar, and M.R. Walter Structural basis for receptor sharing and activation by interleukin-20 receptor-2 (IL-20R2) binding cytokines Proc. Natl. Acad. Sci. U. S. A. 109 31 2012 12704 12709 10.1073/pnas.1117551109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.31 , pp. 12704-12709
    • Logsdon, N.J.1    Deshpande, A.2    Harris, B.D.3    Rajashankar, K.R.4    Walter, M.R.5
  • 38
    • 0031441834 scopus 로고    scopus 로고
    • Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach
    • S. Najjam, R.V. Gibbs, M.Y. Gordon, and C.C. Rider Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach Cytokine 9 12 1997 1013 1022 10.1006/cyto.1997.0246
    • (1997) Cytokine , vol.9 , Issue.12 , pp. 1013-1022
    • Najjam, S.1    Gibbs, R.V.2    Gordon, M.Y.3    Rider, C.C.4
  • 39
    • 0031798591 scopus 로고    scopus 로고
    • Further characterization of the binding of human recombinant interleukin 2 to heparin and identification of putative binding sites
    • S. Najjam, B. Mulloy, J. Theze, M. Gordon, R. Gibbs, and C.C. Rider Further characterization of the binding of human recombinant interleukin 2 to heparin and identification of putative binding sites Glycobiology 8 5 1998 509 516
    • (1998) Glycobiology , vol.8 , Issue.5 , pp. 509-516
    • Najjam, S.1    Mulloy, B.2    Theze, J.3    Gordon, M.4    Gibbs, R.5    Rider, C.C.6
  • 40
    • 0031906297 scopus 로고    scopus 로고
    • Interleukin/5 binds to heparin/heparan sulfate. A model for an interaction with extracellular matrix
    • R.J. Lipscombe, A.M. Nakhoul, C.J. Sanderson, and D.R. Coombe Interleukin/5 binds to heparin/heparan sulfate. A model for an interaction with extracellular matrix J. Leukoc. Biol. 63 3 1998 342 350
    • (1998) J. Leukoc. Biol. , vol.63 , Issue.3 , pp. 342-350
    • Lipscombe, R.J.1    Nakhoul, A.M.2    Sanderson, C.J.3    Coombe, D.R.4


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