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Volumn 159, Issue 2, 1997, Pages 703-711

Different Modes of Peptide Interaction Enable HLA-DQ and HLA-DR Molecules to Bind Diverse Peptide Repertoires

Author keywords

[No Author keywords available]

Indexed keywords

HLA DQ ANTIGEN; HLA DR ANTIGEN; PEPTIDE;

EID: 0031570937     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (51)

References (40)
  • 1
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain, R. N. 1994. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell 76:287.
    • (1994) Cell , vol.76 , pp. 287
    • Germain, R.N.1
  • 2
    • 0029038178 scopus 로고
    • New methods to predict MHC-binding sequences within protein antigens
    • Hammer, J. 1995. New methods to predict MHC-binding sequences within protein antigens. Curr. Opin. Immunol. 7:263.
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 263
    • Hammer, J.1
  • 3
    • 0030930763 scopus 로고    scopus 로고
    • HLA class II peptide binding specificity and autoimmunity
    • In press
    • Hammer, J., T. Sturniolo, and F. Sinigaglia. HLA class II peptide binding specificity and autoimmunity. Adv. Immunol. In press.
    • Adv. Immunol.
    • Hammer, J.1    Sturniolo, T.2    Sinigaglia, F.3
  • 5
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an Influenza virus peptide
    • Stern, L. J., J. H. Brown, T. S. Jardetzky, J. C. Gorga, R. G. Urban, J. L. Strominger, and D. C. Wiley. 1994. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an Influenza virus peptide. Nature 368:215.
    • (1994) Nature , vol.368 , pp. 215
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 6
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • Ghosh, P., M. Amaya, E. Mellins, and D. C. Wiley. 1995. The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378:457.
    • (1995) Nature , vol.378 , pp. 457
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 7
    • 0023257028 scopus 로고
    • Structural characteristics of an antigen required for its interaction with Ia and recognition by T cells
    • Sette, A., S. Buus, S. Colon, J. A. Smith, C. Miles, and H. M. Grey. 1987. Structural characteristics of an antigen required for its interaction with Ia and recognition by T cells. Nature 328:395.
    • (1987) Nature , vol.328 , pp. 395
    • Sette, A.1    Buus, S.2    Colon, S.3    Smith, J.A.4    Miles, C.5    Grey, H.M.6
  • 8
    • 0025911632 scopus 로고
    • Interaction betwenn immunogenic peptides and MHC proteins
    • Rothbard, J. B., and M. L. Gefter. 1991. Interaction betwenn immunogenic peptides and MHC proteins. Annu. Rev. Immunol. 9:527.
    • (1991) Annu. Rev. Immunol. , vol.9 , pp. 527
    • Rothbard, J.B.1    Gefter, M.L.2
  • 10
    • 0025855156 scopus 로고
    • Allele specific motifs revealed by sequencing of self peptides eluted from MHC molecules
    • Falk, K., O. Rotzschke, S. Stevanovic, G. Jung, and H.-G. Rammensee. 1991. Allele specific motifs revealed by sequencing of self peptides eluted from MHC molecules. Nature 351:290.
    • (1991) Nature , vol.351 , pp. 290
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 12
    • 0025369192 scopus 로고
    • Peptide binding to HLA-DR1: A peptide with most residues substituted to alanine retains MHC binding
    • Jardetzky, T. S., J. C. Gorga, R. Busch, J. B. Rothbard, J. L. Strominger, and D. C. Wiley. 1990. Peptide binding to HLA-DR1: a peptide with most residues substituted to alanine retains MHC binding. EMBO J. 9:1797.
    • (1990) EMBO J. , vol.9 , pp. 1797
    • Jardetzky, T.S.1    Gorga, J.C.2    Busch, R.3    Rothbard, J.B.4    Strominger, J.L.5    Wiley, D.C.6
  • 14
    • 0026733530 scopus 로고
    • Functional analysis of DR17(DR3)-restricted mycobacterial T cell epitopes reveals DR17-binding motif and enables the design of allele-specific competitor peptides
    • Geluk, A., K. E. Meijgaarden, A. A. M. Janson, J. W. Drijfhout, R. H. Meloen, R. R. P. Vries, and T. H. M. Ottenhof. 1992. Functional analysis of DR17(DR3)-restricted mycobacterial T cell epitopes reveals DR17-binding motif and enables the design of allele-specific competitor peptides. J. Immunol. 149:2864.
    • (1992) J. Immunol. , vol.149 , pp. 2864
    • Geluk, A.1    Meijgaarden, K.E.2    Janson, A.A.M.3    Drijfhout, J.W.4    Meloen, R.H.5    Vries, R.R.P.6    Ottenhof, T.H.M.7
  • 16
    • 0026706746 scopus 로고
    • Identification of a motif for HLA-DR1 binding peptides using M13 display libraries
    • Hammer, J., B. Takacs, and F. Sinigaglia. 1992. Identification of a motif for HLA-DR1 binding peptides using M13 display libraries. J. Exp. Med. 176:1007.
    • (1992) J. Exp. Med. , vol.176 , pp. 1007
    • Hammer, J.1    Takacs, B.2    Sinigaglia, F.3
  • 19
    • 0027937713 scopus 로고
    • Precise prediction of major histocompatibility complex class II peptide interaction based on peptide side chain scanning
    • Hammer, J., E. Bono, F. Gallazzi, C. Belunis, Z. Nagy, and F. Sinigaglia. 1994. Precise prediction of major histocompatibility complex class II peptide interaction based on peptide side chain scanning. J. Exp. Med. 180:2353.
    • (1994) J. Exp. Med. , vol.180 , pp. 2353
    • Hammer, J.1    Bono, E.2    Gallazzi, F.3    Belunis, C.4    Nagy, Z.5    Sinigaglia, F.6
  • 20
    • 0027243171 scopus 로고
    • The importance of dominant negative effects of amino acid side chain substitution in peptide-MHC molecule interactions and T cell recognition
    • Boehncke, W. H., T. Takeshita, C. D. Pendleton, R. A. Houghten, N. Sadegh, S. Racioppi, J. A. Berzofsky, and R. N. Germain. 1993. The importance of dominant negative effects of amino acid side chain substitution in peptide-MHC molecule interactions and T cell recognition. J. Immunol. 150:331.
    • (1993) J. Immunol. , vol.150 , pp. 331
    • Boehncke, W.H.1    Takeshita, T.2    Pendleton, C.D.3    Houghten, R.A.4    Sadegh, N.5    Racioppi, S.6    Berzofsky, J.A.7    Germain, R.N.8
  • 22
    • 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., R. M. Kantor, and M. M. Davis. 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.
    • (1994) J. Immunol. , vol.152 , pp. 3946
    • Reay, P.A.1    Kantor, R.M.2    Davis, M.M.3
  • 23
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains
    • Parker, K. C., M. A. Bednarek, and J. E. Coligan. 1994. Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains. J. Immunol. 152:163.
    • (1994) J. Immunol. , vol.152 , pp. 163
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 24
    • 0029932708 scopus 로고    scopus 로고
    • Specificity of an HLA-DRB1*0401 restricted T cell response to type II collagen
    • Fugger, L., J. Rothbard, and G. Sonderstrup-McDevitt. 1996. Specificity of an HLA-DRB1*0401 restricted T cell response to type II collagen. Eur. J. Immunol. 26:928.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 928
    • Fugger, L.1    Rothbard, J.2    Sonderstrup-McDevitt, G.3
  • 26
    • 0029823313 scopus 로고    scopus 로고
    • Both alpha and beta chain polymorphisms determine the specificity of the disease-associated HLA-DQ molecules, with beta chain residues being most influential
    • Johansen, B. H., T. Jensen, C. J. Thorpe, F. Vartdal, E. Thorsby, and L. M. Sollid. 1996. Both alpha and beta chain polymorphisms determine the specificity of the disease-associated HLA-DQ molecules, with beta chain residues being most influential. Immunogenetics 45:142.
    • (1996) Immunogenetics , vol.45 , pp. 142
    • Johansen, B.H.1    Jensen, T.2    Thorpe, C.J.3    Vartdal, F.4    Thorsby, E.5    Sollid, L.M.6
  • 27
    • 0029979525 scopus 로고    scopus 로고
    • Allele-specific motifs characterize HLA-DQ interaction with a Diabetes-associated peptide derived from glutamic acid decarboxylase
    • Kwok, W. W., M. E. Domeier, F. C. Raymond, P. Byers, and G. T. Nepom. 1996. Allele-specific motifs characterize HLA-DQ interaction with a Diabetes-associated peptide derived from glutamic acid decarboxylase. J. Immunol. 156:2171.
    • (1996) J. Immunol. , vol.156 , pp. 2171
    • Kwok, W.W.1    Domeier, M.E.2    Raymond, F.C.3    Byers, P.4    Nepom, G.T.5
  • 30
    • 0029815574 scopus 로고    scopus 로고
    • Peptide binding characteristics of the coeliac disease-associated DQ(α1*0501, β1*0201) molecule
    • Van de Wal, Y., Y. M. C. Kooy, J. W. Drijfhout, R. Amons, and F. Koning. 1996. Peptide binding characteristics of the coeliac disease-associated DQ(α1*0501, β1*0201) molecule. Immunogenetics 44:246.
    • (1996) Immunogenetics , vol.44 , pp. 246
    • Van De Wal, Y.1    Kooy, Y.M.C.2    Drijfhout, J.W.3    Amons, R.4    Koning, F.5
  • 31
    • 0029450142 scopus 로고
    • Binding domain regulation of MHC class III molecule assembly, trafficking, fate, and function
    • Germain, R. N. 1995. Binding domain regulation of MHC class III molecule assembly, trafficking, fate, and function. Semin. Immunol. 7:361.
    • (1995) Semin. Immunol. , vol.7 , pp. 361
    • Germain, R.N.1
  • 35
    • 0024796883 scopus 로고
    • Universally immunogenic T cell epitopes: Promiscuous binding to human MHC class II and promiscuous recognition by T cells
    • Panina-Bordignon, P., A. Tan, A. Termijtelen, S. Demotz, G. Corradin, and A. Lanzavecchia. 1989. Universally immunogenic T cell epitopes: promiscuous binding to human MHC class II and promiscuous recognition by T cells. Eur. J. Immunol. 19:2237.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2237
    • Panina-Bordignon, P.1    Tan, A.2    Termijtelen, A.3    Demotz, S.4    Corradin, G.5    Lanzavecchia, A.6
  • 37
    • 0028800411 scopus 로고
    • CLIP binds to HLA class II using methionine-based, allele-dependent motifs as well as allele-independent supermotifs
    • Geluk, A., K. E. Vanmeijgaarden, J. W. Drijfhout, and T. H. M. Ottenhoff. 1995. CLIP binds to HLA class II using methionine-based, allele-dependent motifs as well as allele-independent supermotifs. Mol. Immunol. 32:975.
    • (1995) Mol. Immunol. , vol.32 , pp. 975
    • Geluk, A.1    Vanmeijgaarden, K.E.2    Drijfhout, J.W.3    Ottenhoff, T.H.M.4
  • 38
    • 0028945021 scopus 로고
    • Supermotifs enable natural invariant chain-derived peptides to interact with many major histocompatibility complex-class II molecules
    • Malcherek, G., V. Gnau, G. Jung, H. G. Rammensee, and A. Melms. 1995. Supermotifs enable natural invariant chain-derived peptides to interact with many major histocompatibility complex-class II molecules. J. Exp. Med. 181:527.
    • (1995) J. Exp. Med. , vol.181 , pp. 527
    • Malcherek, G.1    Gnau, V.2    Jung, G.3    Rammensee, H.G.4    Melms, A.5
  • 39
    • 0028921633 scopus 로고
    • Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II
    • Sette, A., S. Southwood, J. Miller, and E. Appella. 1995. Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II. J. Exp. Med. 181:677.
    • (1995) J. Exp. Med. , vol.181 , pp. 677
    • Sette, A.1    Southwood, S.2    Miller, J.3    Appella, E.4


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