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Volumn 10, Issue 1, 1999, Pages 51-61

Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; T LYMPHOCYTE RECEPTOR;

EID: 0033024354     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-7613(00)80006-0     Document Type: Article
Times cited : (120)

References (73)
  • 6
    • 0032511415 scopus 로고    scopus 로고
    • T cells recognize a glycopeptide derived from type II collagen in a model for rheumatoid arthritis
    • Broddefalk, J., Backlund, J., Almqvist, F., Johansson, M., Holmdahl, R., and Kihlberg, J. (1998). T cells recognize a glycopeptide derived from type II collagen in a model for rheumatoid arthritis. J. Am. Chem. Soc. 120, 7676-7683.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7676-7683
    • Broddefalk, J.1    Backlund, J.2    Almqvist, F.3    Johansson, M.4    Holmdahl, R.5    Kihlberg, J.6
  • 7
    • 0030767713 scopus 로고    scopus 로고
    • The free R value: A more objective statistic for crystallography
    • Brünger, A.T. (1997). The free R value: A more objective statistic for crystallography. Methods Enzymol. 277, 366-396.
    • (1997) Methods Enzymol. , vol.277 , pp. 366-396
    • Brünger, A.T.1
  • 8
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J., and Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 9
    • 0030928027 scopus 로고    scopus 로고
    • Carbohydrates and antigen recognition by T cells
    • Carbone, F.R., and Gleeson, P.A. (1997). Carbohydrates and antigen recognition by T cells. Glycobiology 7, 725-730.
    • (1997) Glycobiology , vol.7 , pp. 725-730
    • Carbone, F.R.1    Gleeson, P.A.2
  • 12
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M.L. (1983). Solvent-accessible surfaces of proteins and nucleic acids. Science 221, 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 13
    • 0029040102 scopus 로고
    • Issues concerning the nature of antigen recognition by αβ and γδ T cell receptors
    • Davis, M.M., and Chien, Y. (1995). Issues concerning the nature of antigen recognition by αβ and γδ T cell receptors. Immunol. Today 16, 316-318.
    • (1995) Immunol. Today , vol.16 , pp. 316-318
    • Davis, M.M.1    Chien, Y.2
  • 15
    • 18344405559 scopus 로고    scopus 로고
    • Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids
    • Ding, Y.H., Smith, K.J., Garboczi, D.N., Utz, U., Biddison, W.E., and Wiley, D.C. (1998). Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity 8, 403-411.
    • (1998) Immunity , vol.8 , pp. 403-411
    • Ding, Y.H.1    Smith, K.J.2    Garboczi, D.N.3    Utz, U.4    Biddison, W.E.5    Wiley, D.C.6
  • 16
    • 0029805829 scopus 로고    scopus 로고
    • Antigen-specific t-cell receptors and their reactions with complexes formed by peptides with major histocompatibility complex proteins
    • Eisen, H.N., Sykulev, Y., and Tsomides, T.J. (1996). Antigen-specific t-cell receptors and their reactions with complexes formed by peptides with major histocompatibility complex proteins. Adv. Protein Chem. 49, 1-56.
    • (1996) Adv. Protein Chem. , vol.49 , pp. 1-56
    • Eisen, H.N.1    Sykulev, Y.2    Tsomides, T.J.3
  • 19
    • 0030854842 scopus 로고    scopus 로고
    • T-cell recognition of tumor-associated carbohydrates: The nature of the glycan moiety plays a decisive role in determining glycopeptide immunogenicity
    • Galli-Stampino, L., Meinjohanns, E., Frische, K., Meldal, M., Jensen, T., Werdelin, O., and Mouritsen, S. (1997). T-cell recognition of tumor-associated carbohydrates: The nature of the glycan moiety plays a decisive role in determining glycopeptide immunogenicity. Cancer Res. 57, 3214-3222.
    • (1997) Cancer Res. , vol.57 , pp. 3214-3222
    • Galli-Stampino, L.1    Meinjohanns, E.2    Frische, K.3    Meldal, M.4    Jensen, T.5    Werdelin, O.6    Mouritsen, S.7
  • 20
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human t-cell receptor, viral peptide and HLA-A2
    • Garboczi, D.N., Ghosh, P., Utz, U., Fan, Q.R., Biddison, W.E., and Wiley, D.C. (1996). Structure of the complex between human t-cell receptor, viral peptide and HLA-A2. Nature 384, 134-141.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 22
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in t-cell receptor recognition of a self peptide-MHC antigen
    • Garcia, K.C., Degano, M., Pease, L.R., Huang, M., Peterson, P.A., Teyton, L., and Wilson, I.A. (1998). Structural basis of plasticity in t-cell receptor recognition of a self peptide-MHC antigen. Science 279, 1166-1172.
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1    Degano, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5    Teyton, L.6    Wilson, I.A.7
  • 23
    • 0002995958 scopus 로고
    • General concept of tumor-associated carbohydrate antigens: Their chemical, physical, and enzymatic basis
    • H.F. Oettgen, ed. (Weinheim, Germany: VCH)
    • Hakomori, S. (1989). General concept of tumor-associated carbohydrate antigens: Their chemical, physical, and enzymatic basis. In Gangliosides and Cancer, H.F. Oettgen, ed. (Weinheim, Germany: VCH), pp. 57-68.
    • (1989) In Gangliosides and Cancer , pp. 57-68
    • Hakomori, S.1
  • 24
    • 0025315127 scopus 로고
    • Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: Peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization
    • Hansen, J.E., Clausen, H., Nielsen, C., Teglbjaerg, L.S., Hansen, L.L., Nielsen, C.M., Dabelsteen, E., Mathiesen, L., Hakomori, S.I., and Nielsen, J.O. (1990). Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: Peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization. J. Virol. 64, 2833-2840.
    • (1990) J. Virol. , vol.64 , pp. 2833-2840
    • Hansen, J.E.1    Clausen, H.2    Nielsen, C.3    Teglbjaerg, L.S.4    Hansen, L.L.5    Nielsen, C.M.6    Dabelsteen, E.7    Mathiesen, L.8    Hakomori, S.I.9    Nielsen, J.O.10
  • 26
    • 0028318850 scopus 로고
    • Recognition of carbohydrate by major histocompatibility complex class i-restricted, glycopeptide-specific cytotoxic T lymphocytes
    • Haurum, J.S., Arsequell, G., Lellouch, A.C., Wong, S.Y., Dwek, R.A., McMichael, A.J., and Elliott, T. (1994). Recognition of carbohydrate by major histocompatibility complex class i-restricted, glycopeptide-specific cytotoxic T lymphocytes. J. Exp. Med. 180, 739-744.
    • (1994) J. Exp. Med. , vol.180 , pp. 739-744
    • Haurum, J.S.1    Arsequell, G.2    Lellouch, A.C.3    Wong, S.Y.4    Dwek, R.A.5    McMichael, A.J.6    Elliott, T.7
  • 28
    • 0023634937 scopus 로고
    • Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonie adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β(1-3) N-acetylglucosaminyltransferase
    • Holmes, E.H., Hakomori, S., and Ostrander, G.K. (1987). Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonie adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β(1-3) N-acetylglucosaminyltransferase. J. Biol. Chem. 262, 15649-15658.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15649-15658
    • Holmes, E.H.1    Hakomori, S.2    Ostrander, G.K.3
  • 29
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF-a program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G., and Thornton, J.M. (1996). Promotif-a program to identify and analyze structural motifs in proteins. Prot. Sci. 5, 212-220.
    • (1996) Prot. Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 31
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Cowan, S., Zou, J.Y., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
    • (1991) Acta Cryst. , vol.47 A , pp. 110-119
    • Jones, T.A.1    Cowan, S.2    Zou, J.Y.3    Kjeldgaard, M.4
  • 32
    • 0029864606 scopus 로고    scopus 로고
    • γδ and other unconventional T lymphocytes: What do they see and what do they do?
    • Kaufmann, S.H. (1996). γδ and other unconventional T lymphocytes: What do they see and what do they do? Proc. Natl. Acad. Sci. USA 93, 2272-2279.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2272-2279
    • Kaufmann, S.H.1
  • 33
    • 0031008551 scopus 로고    scopus 로고
    • Solid-phase synthesis of glycopeptides: Immunological studies with T cell stimulating glycopeptides
    • Kihlberg, J., and Elofsson, M. (1997). Solid-phase synthesis of glycopeptides: Immunological studies with T cell stimulating glycopeptides. Curr. Med. Chem. 4, 85-116.
    • (1997) Curr. Med. Chem. , vol.4 , pp. 85-116
    • Kihlberg, J.1    Elofsson, M.2
  • 34
    • 0002738008 scopus 로고
    • Dictionaries for heteros
    • Kleywegt, G.J. (1995). Dictionaries for heteros. ESF/CCP4 Newsletter 31, 45-50.
    • (1995) ESF/CCP4 Newsletter , vol.31 , pp. 45-50
    • Kleywegt, G.J.1
  • 35
    • 0030845843 scopus 로고    scopus 로고
    • Model building and refinement practice
    • Kleywegt, G.J., and Jones, T.A. (1997). Model building and refinement practice. Methods Enzymol. 277, 208-230.
    • (1997) Methods Enzymol. , vol.277 , pp. 208-230
    • Kleywegt, G.J.1    Jones, T.A.2
  • 36
    • 0031568083 scopus 로고    scopus 로고
    • Carrier-independent hapten recognition and promiscuous MHC restriction by CD4 T cells induced by trinitrophenylated peptides
    • Kohler, J., Hartmann, U., Grimm, R., Pflugfelder, U., and Weltzien, H.U. (1997). Carrier-independent hapten recognition and promiscuous MHC restriction by CD4 T cells induced by trinitrophenylated peptides. J. Immunol. 158, 591-597.
    • (1997) J. Immunol. , vol.158 , pp. 591-597
    • Kohler, J.1    Hartmann, U.2    Grimm, R.3    Pflugfelder, U.4    Weltzien, H.U.5
  • 37
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R., and Kornfeld, S. (1985). Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 38
    • 0027595079 scopus 로고
    • Identifying strategies for immune intervention
    • Lanzavecchia, A. (1993). Identifying strategies for immune intervention. Science 260, 937-944.
    • (1993) Science , vol.260 , pp. 937-944
    • Lanzavecchia, A.1
  • 39
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. (1952). Traitement statistique des erreurs dans la determination des structures cristallines. Acta Cryst. 5, 802-810.
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 41
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden, D.R., Garboczi, D.N., and Wiley, D.C. (1993). The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75, 693-708.
    • (1993) Cell , vol.75 , pp. 693-708
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 42
    • 0026666103 scopus 로고
    • Role of hapten-anchoring peptides in defining haptenepitopes for MHC-restricted cytotoxic T cells. Cross-reactive TNP-determinants on different peptides
    • Martin, S., Ortmann, B., Pflugfelder, U., Birsner, U., and Weltzien, H.U. (1992). Role of hapten-anchoring peptides in defining haptenepitopes for MHC-restricted cytotoxic T cells. Cross-reactive TNP-determinants on different peptides. J. Immunol. 149, 2569-2575.
    • (1992) J. Immunol. , vol.149 , pp. 2569-2575
    • Martin, S.1    Ortmann, B.2    Pflugfelder, U.3    Birsner, U.4    Weltzien, H.U.5
  • 43
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 44
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I.K., and Thornton, J.M. (1994). Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 47
    • 0023618696 scopus 로고
    • Density-dependent recognition of cell surface GM3 by a certain antimelanoma antibody, and GM3 lactone as a possible immunogen: Requirements for tumor-associated antigen and immunogen
    • Nores, G.A., Dohi, T., Taniguchi, M., and Hakomori, S. (1987). Density-dependent recognition of cell surface GM3 by a certain antimelanoma antibody, and GM3 lactone as a possible immunogen: Requirements for tumor-associated antigen and immunogen. J. Immunol. 139, 3171-3176.
    • (1987) J. Immunol. , vol.139 , pp. 3171-3176
    • Nores, G.A.1    Dohi, T.2    Taniguchi, M.3    Hakomori, S.4
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 0027399243 scopus 로고
    • Peptides naturally presented by MHC class I molecules
    • Rammensee, H.G., Falk, K., and Rotzschke, O. (1993). Peptides naturally presented by MHC class I molecules. Annu. Rev. Immunol. 11, 213-244.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 213-244
    • Rammensee, H.G.1    Falk, K.2    Rotzschke, O.3
  • 53
    • 0028985984 scopus 로고
    • MHC ligands and peptide motifs: First listing
    • Rammensee, H.G., Friede, T., and Stevanoviic, S. (1995). MHC ligands and peptide motifs: First listing. Immunogenetics 41,178-228.
    • (1995) Immunogenetics , vol.41 , pp. 178-228
    • Rammensee, H.G.1    Friede, T.2    Stevanoviic, S.3
  • 54
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A42,140-149.
    • (1986) Acta Cryst. , vol.42 A , pp. 140-149
    • Read, R.J.1
  • 56
    • 0028069388 scopus 로고
    • CDR3 length in antigen-specific immune receptors
    • Rock, E.P., Sibbald, P.R., Davis, M.M., and Chien, Y.H. (1994). CDR3 length in antigen-specific immune receptors. J. Exp. Med. 179, 323-328.
    • (1994) J. Exp. Med. , vol.179 , pp. 323-328
    • Rock, E.P.1    Sibbald, P.R.2    Davis, M.M.3    Chien, Y.H.4
  • 58
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G.M., and Schneider, T.R. (1997). SHELXL: High-resolution refinement. Methods Enzymol. 277, 319-343.
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 59
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3Å resolution
    • Sheriff, S., Hendrickson, W.A., and Smith, J.L. (1987). Structure of myohemerythrin in the azidomet state at 1.7/1.3Å resolution. J. Mol. Biol. 197, 273-296.
    • (1987) J. Mol. Biol. , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3
  • 61
    • 0029969665 scopus 로고    scopus 로고
    • Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53
    • Smith, K.J., Reid, S.W., Harlos, K., McMichael, A.J., Stuart, D.I., Bell, J.I., and Jones, E.Y. (1996a). Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity 4, 215-228.
    • (1996) Immunity , vol.4 , pp. 215-228
    • Smith, K.J.1    Reid, S.W.2    Harlos, K.3    McMichael, A.J.4    Stuart, D.I.5    Bell, J.I.6    Jones, E.Y.7
  • 63
    • 0029032964 scopus 로고
    • Molview: A program for analyzing and displaying atomic structures on the macintosh personal computer
    • Smith, T.J. (1995). Molview: A program for analyzing and displaying atomic structures on the macintosh personal computer. J. Mol. Graph. 13, 122-125.
    • (1995) J. Mol. Graph. , vol.13 , pp. 122-125
    • Smith, T.J.1
  • 66
    • 0023048923 scopus 로고
    • X-ray crystal structure of galabiose, O-α-D-galactopyranosyl-(1-4)-D-galactopyranose
    • Svensson, G., Albertsson, J., Svensson, C., Magnusson, G., and Dahmen, J. (1986). X-ray crystal structure of galabiose, O-α-D-galactopyranosyl-(1-4)-D-galactopyranose. Carbohydr. Res. 146, 29-38.
    • (1986) Carbohydr. Res. , vol.146 , pp. 29-38
    • Svensson, G.1    Albertsson, J.2    Svensson, C.3    Magnusson, G.4    Dahmen, J.5
  • 68
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993). Biological roles of oligosaccharides: All of the theories are correct. Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 69
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson, I.A., and Stanfield, R.L. (1994). Antibody-antigen interactions: New structures and new conformational changes. Curr. Opin. Struct. Biol. 4, 857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 70
    • 0344193129 scopus 로고    scopus 로고
    • T cell receptor structure and TCR complexes
    • Wilson, I.A., and Garcia, K.C. (1997). T cell receptor structure and TCR complexes. Curr. Opin. Struct. Biol. 7, 839-848.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 839-848
    • Wilson, I.A.1    Garcia, K.C.2
  • 72
    • 0030826423 scopus 로고    scopus 로고
    • Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove
    • Zeng, Z., Castaño, A.R., Segelke, B.W., Stura, E.A., Peterson, P.A., and Wilson, I.A. (1997). Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove. Science 277, 339-345.
    • (1997) Science , vol.277 , pp. 339-345
    • Zeng, Z.1    Castaño, A.R.2    Segelke, B.W.3    Stura, E.A.4    Peterson, P.A.5    Wilson, I.A.6
  • 73
    • 0026657070 scopus 로고
    • In vivo primary induction of virus-specific CTL by immunization with 9mer synthetic peptides
    • Zhou, X., Berg, L., Motal, U.M., and Jondal, M. (1992). In vivo primary induction of virus-specific CTL by immunization with 9mer synthetic peptides. J. Immunol. Methods 153, 193-200.
    • (1992) J. Immunol. Methods , vol.153 , pp. 193-200
    • Zhou, X.1    Berg, L.2    Motal, U.M.3    Jondal, M.4


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