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Volumn 8, Issue 3, 1998, Pages 305-317

Crystal structure of I-A(k) in complex with a dominant epitope of lysozyme

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; LYSOZYME; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PEPTIDE; T LYMPHOCYTE RECEPTOR;

EID: 0032033445     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-7613(00)80536-1     Document Type: Article
Times cited : (225)

References (50)
  • 1
    • 0003403213 scopus 로고
    • The first external domain of the non-obese diabetic mouse class II I-A beta chain is unique
    • Acha-Orbea, H., and McDevitt, H.O. (1987). The first external domain of the non-obese diabetic mouse class II I-A beta chain is unique. Proc. Natl. Acad. Sci USA 84, 2435-2442.
    • (1987) Proc. Natl. Acad. Sci USA , vol.84 , pp. 2435-2442
    • Acha-Orbea, H.1    McDevitt, H.O.2
  • 2
    • 0024206747 scopus 로고
    • Mechanisms influencing the immunodominance of T cell determinants
    • Adorini, L., Appella, E., Doria, G., and Nagy, Z.A. (1988). Mechanisms influencing the immunodominance of T cell determinants. J. Exp. Med. 168, 2091-2104.
    • (1988) J. Exp. Med. , vol.168 , pp. 2091-2104
    • Adorini, L.1    Appella, E.2    Doria, G.3    Nagy, Z.A.4
  • 3
    • 0021360513 scopus 로고
    • Differential requirements for antigen processing by macrophages for lysozyme-specific T cell hybridomas
    • Allen, P.M., and Unanue, E.R. (1984). Differential requirements for antigen processing by macrophages for lysozyme-specific T cell hybridomas. J. Immunol. 132, 1077-1079.
    • (1984) J. Immunol. , vol.132 , pp. 1077-1079
    • Allen, P.M.1    Unanue, E.R.2
  • 4
  • 5
    • 0021968677 scopus 로고
    • Binding of immunogenic peptides to Ia histocompatibility molecules
    • Babbitt, B.P., Allen, P.M., Matsueda, G., Haber, E., and Unanue, E.R. (1985). Binding of immunogenic peptides to Ia histocompatibility molecules. Nature 317, 359-361.
    • (1985) Nature , vol.317 , pp. 359-361
    • Babbitt, B.P.1    Allen, P.M.2    Matsueda, G.3    Haber, E.4    Unanue, E.R.5
  • 7
    • 0023115557 scopus 로고
    • The relation between major histocompatibility complex (MHC) restriction and the capacity of Ia to bind immunogenic peptides
    • Buus, S., Sette, A., Colon, S.M., Miles, C., and Grey, H.M. (1987). The relation between major histocompatibility complex (MHC) restriction and the capacity of Ia to bind immunogenic peptides. Science 235, 1353-1358.
    • (1987) Science , vol.235 , pp. 1353-1358
    • Buus, S.1    Sette, A.2    Colon, S.M.3    Miles, C.4    Grey, H.M.5
  • 8
    • 0023140814 scopus 로고
    • Crystallographic R-factor refinement by molecular dynamics
    • Brunger, 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
    • Brunger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 9
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M. (1987). Ribbon models of macromolecules. J. Mol. Graphics 5, 103-106.
    • (1987) J. Mol. Graphics , vol.5 , pp. 103-106
    • Carson, M.1
  • 10
    • 0030802693 scopus 로고    scopus 로고
    • T cell receptor recognition of MHC class II-bound peptide flanking residues enhances immunogenicity and results in altered TcR V region usage
    • Carson, R.T., Vignali, K.M., Woodland, D.L., and Vignali, D.A. (1997). T cell receptor recognition of MHC class II-bound peptide flanking residues enhances immunogenicity and results in altered TcR V region usage. Immunity 7, 387-400.
    • (1997) Immunity , vol.7 , pp. 387-400
    • Carson, R.T.1    Vignali, K.M.2    Woodland, D.L.3    Vignali, D.A.4
  • 11
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly, M.L. (1993). The molecular surface package. J. Mol. Graphics 11, 139-141.
    • (1993) J. Mol. Graphics , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 12
    • 0026734985 scopus 로고
    • Evaluation of the functional equivalence of major histocompatible complex class II A and E complexes
    • Cosgrove, D., Bodmer, H., Bogue, M., Benoist, C., and Mathis, D. (1992). Evaluation of the functional equivalence of major histocompatible complex class II A and E complexes. J. Exp. Med. 176, 629-634.
    • (1992) J. Exp. Med. , vol.176 , pp. 629-634
    • Cosgrove, D.1    Bodmer, H.2    Bogue, M.3    Benoist, C.4    Mathis, D.5
  • 13
    • 0030745938 scopus 로고    scopus 로고
    • Characterization and quantitation of peptide-MHC complexes produced from hen egg lysozyme using a monoclonal antibody
    • Dadaglio, G., Nelson, C.A., Deck, M.B., Petzold, S.J., and Unanue, E.R. (1997). Characterization and quantitation of peptide-MHC complexes produced from hen egg lysozyme using a monoclonal antibody. Immunity 6, 727-738.
    • (1997) Immunity , vol.6 , pp. 727-738
    • Dadaglio, G.1    Nelson, C.A.2    Deck, M.B.3    Petzold, S.J.4    Unanue, E.R.5
  • 14
    • 0028168468 scopus 로고
    • (His)C epsilon-H...O=C < hydrogen bond in the active sitesof serine hydrolases
    • Derewenda, Z.S., Derewenda, U., and Kobos P.M. (1994). (His)C epsilon-H...O=C < hydrogen bond in the active sitesof serine hydrolases. J. Mol. Biol. 241, 83-93.
    • (1994) J. Mol. Biol. , vol.241 , pp. 83-93
    • Derewenda, Z.S.1    Derewenda, U.2    Kobos, P.M.3
  • 15
    • 0030701632 scopus 로고    scopus 로고
    • X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II
    • Dessen, A., Lawrence, C.M., Cupo, S., Zaller, D.M., and Wiley, D.C. (1997). X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity 7 473-481.
    • (1997) Immunity , vol.7 , pp. 473-481
    • Dessen, A.1    Lawrence, C.M.2    Cupo, S.3    Zaller, D.M.4    Wiley, D.C.5
  • 19
    • 0029782111 scopus 로고    scopus 로고
    • Structures of an MHC class II molecule with covalently bound single peptides
    • Fremont, D.H., Hendrickson, W.A., Marrack, P., and Kappler, J.W. (1996). Structures of an MHC class II molecule with covalently bound single peptides. Science 272, 1001-1004.
    • (1996) Science , vol.272 , pp. 1001-1004
    • Fremont, D.H.1    Hendrickson, W.A.2    Marrack, P.3    Kappler, J.W.4
  • 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
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • Ghosh, P., Amaya, M., Mellins, E., and Wiley, D.C. (1995). The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378, 457-462.
    • (1995) Nature , vol.378 , pp. 457-462
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 23
    • 0025893640 scopus 로고
    • Effects of pH and polysaccharides on peptide binding to class II major histocompatibility complex molecules
    • Harding, C.V., Roof, R.W., Allen, P.M., and Unanue E.R. (1991). Effects of pH and polysaccharides on peptide binding to class II major histocompatibility complex molecules. Proc. Natl. Acad. Sci. USA 88, 2740-2744.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2740-2744
    • Harding, C.V.1    Roof, R.W.2    Allen, P.M.3    Unanue, E.R.4
  • 24
    • 0027497604 scopus 로고
    • How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme
    • Heinz, D.W., Baase, W.A., Dahlquist, F.W., and Matthews, B.W. (1993). How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature 361, 561-564.
    • (1993) Nature , vol.361 , pp. 561-564
    • Heinz, D.W.1    Baase, W.A.2    Dahlquist, F.W.3    Matthews, B.W.4
  • 25
    • 0030069683 scopus 로고    scopus 로고
    • Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides
    • Jardetzky, T.S., Brown, J.H., Gorga, J.C., Stern, L.J., Urban, R.G., Strominger, J.L., and Wiley, D.C. (1996). Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc. Natl. Acad. Sci. USA 93, 734-738.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 734-738
    • Jardetzky, T.S.1    Brown, J.H.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 26
    • 0000356656 scopus 로고
    • A graphical model building and refinement system for macromolecules
    • Jones, T.A. (1978). A graphical model building and refinement system for macromolecules. J. Appl. Crystallogr. 11, 268-272.
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta. Crystallogr. A 47, 110-119.
    • (1991) Acta. Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 30
    • 0028233838 scopus 로고
    • Functional soluble major histocompatibility complex proteins with covalently bound peptides
    • Kozono, H., White, J., Clements, J., Marrack, P., and Kappler, J.W. (1994). Functional soluble major histocompatibility complex proteins with covalently bound peptides. Nature 369, 151-154.
    • (1994) Nature , vol.369 , pp. 151-154
    • Kozono, H.1    White, J.2    Clements, J.3    Marrack, P.4    Kappler, J.W.5
  • 31
    • 0002898158 scopus 로고
    • Phospholipases that degrade the glycosyl-phosphatidyl inositol anchor of membrane proteins
    • N.M. Hooper and A.J. Turner, eds. (New York: Oxford University Press)
    • Low, M.G. (1992). Phospholipases that degrade the glycosyl-phosphatidyl inositol anchor of membrane proteins. In Lipid Modification of Proteins: A Practical Approach, N.M. Hooper and A.J. Turner, eds. (New York: Oxford University Press), pp. 117-154.
    • (1992) Lipid Modification of Proteins: A Practical Approach , pp. 117-154
    • Low, M.G.1
  • 37
    • 0023395438 scopus 로고
    • Major histocompatibility complex gene organization in the mole rat, Spalax ehrenbergi: Evidence for transfer of function between class II genes
    • Nizetic, D., Figueroa, F., Dembic, Z., Nevo, E., and Klein, J. (1987). Major histocompatibility complex gene organization in the mole rat, Spalax ehrenbergi: evidence for transfer of function between class II genes. Proc. Natl. Acad. Sci. USA 84, 5828-5832.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5828-5832
    • Nizetic, D.1    Figueroa, F.2    Dembic, Z.3    Nevo, E.4    Klein, J.5
  • 38
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • 29-30 January, 1993, L. Sawyer, N. Isaacs, and S. Bailey, compilers (Warrington, England: SERC Daresbury Laboratory)
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing, 29-30 January, 1993, L. Sawyer, N. Isaacs, and S. Bailey, compilers (Warrington, England: SERC Daresbury Laboratory), pp. 56-62.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 39
    • 0026643116 scopus 로고
    • pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule
    • Reay, P.A., Wettstein, D.A., and Davis, M.M. (1992). pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule. EMBO J. 11, 2829-2839.
    • (1992) EMBO J. , vol.11 , pp. 2829-2839
    • Reay, P.A.1    Wettstein, D.A.2    Davis, M.M.3
  • 40
    • 0028261582 scopus 로고
    • Use of global amino acid replacements to define the requirements for MHC binding and T-cell recognition of moth cytochrome c (93-103)
    • Reay, P.A., Kantor, R.M., and Davis M.M. (1994). Use of global amino acid replacements to define the requirements for MHC binding and T-cell recognition of moth cytochrome c (93-103). J. Immunol. 152, 3946-3957.
    • (1994) J. Immunol. , vol.152 , pp. 3946-3957
    • Reay, P.A.1    Kantor, R.M.2    Davis, M.M.3
  • 41
    • 0001257560 scopus 로고
    • The beta bulge: A common small unit of nonrepetitive protein structure
    • Richardson, J.S., Getzoff, E.D., and Richardson, D.C. (1978). The beta bulge: a common small unit of nonrepetitive protein structure. Proc. Natl. Acad. Sci. USA 75, 2574-2578.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2574-2578
    • Richardson, J.S.1    Getzoff, E.D.2    Richardson, D.C.3
  • 43
    • 0023449784 scopus 로고
    • Predominant role of amino-terminal sequences in dictating efficiency of class II major histocompatibility complex alpha beta dimer expression
    • Sant, A.J., Braunstein, N.S., and Germain, R.N. (1987). Predominant role of amino-terminal sequences in dictating efficiency of class II major histocompatibility complex alpha beta dimer expression. Proc. Natl. Acad. Sci. USA 84, 8065-8069.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8065-8069
    • Sant, A.J.1    Braunstein, N.S.2    Germain, R.N.3
  • 45
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • Smith, K.J., Reid, S.W., Stuart, D.I., McMichael, A.J., Jones, E.Y., and Bell, J.I. (1996). An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4, 203-213.
    • (1996) Immunity , vol.4 , pp. 203-213
    • Smith, K.J.1    Reid, S.W.2    Stuart, D.I.3    McMichael, A.J.4    Jones, E.Y.5    Bell, J.I.6
  • 46
    • 0027134809 scopus 로고
    • Expression and function of mixed isotype MHC class II molecules in normal mice
    • Spencer, J.S., Freed, J.H., and Kubo, R.T. (1993). Expression and function of mixed isotype MHC class II molecules in normal mice. J. Immunol. 151, 6822-6832.
    • (1993) J. Immunol. , vol.151 , pp. 6822-6832
    • Spencer, J.S.1    Freed, J.H.2    Kubo, R.T.3
  • 47
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an antigenic peptide from influenza virus
    • Stern, L., Brown, G., Jardetzky, T., Gorga, J., Urban, R., Strominger, J., and Wiley, D. (1994). Crystal structure of the human class II MHC protein HLA-DR1 complexed with an antigenic peptide from influenza virus. Nature 368, 215-221.
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.1    Brown, G.2    Jardetzky, T.3    Gorga, J.4    Urban, R.5    Strominger, J.6    Wiley, D.7
  • 48
    • 0023252262 scopus 로고
    • HLA-DQ beta gene contributes to susceptibility and resistance to insulin-dependent diabetes mellitus
    • Todd, J.A., Bell, J.I., and McDevitt, H.O. (1987). HLA-DQ beta gene contributes to susceptibility and resistance to insulin-dependent diabetes mellitus. Nature 329,599-602.
    • (1987) Nature , vol.329 , pp. 599-602
    • Todd, J.A.1    Bell, J.I.2    McDevitt, H.O.3
  • 49
    • 0029937756 scopus 로고    scopus 로고
    • Complexes generated by the binding of free peptides to class II MHC molecules are antigenically diverse compared with those generated by intracellular processing
    • Viner, N.J., Nelson, C.A., Deck, B., and Unanue, E.R. (1996). Complexes generated by the binding of free peptides to class II MHC molecules are antigenically diverse compared with those generated by intracellular processing. J. Immunol. 156, 2365-2368.
    • (1996) J. Immunol. , vol.156 , pp. 2365-2368
    • Viner, N.J.1    Nelson, C.A.2    Deck, B.3    Unanue, E.R.4
  • 50
    • 0025898515 scopus 로고
    • Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH
    • Wettstein, D.A., Boniface, J.J., Reay, P.A., Schild, H., and Davis, M.M. (1991). Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH. J. Exp. Med. 174, 219-228.
    • (1991) J. Exp. Med. , vol.174 , pp. 219-228
    • Wettstein, D.A.1    Boniface, J.J.2    Reay, P.A.3    Schild, H.4    Davis, M.M.5


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