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Volumn 176, Issue 5, 2006, Pages 2958-2968

Amino-terminal flanking residues determine the conformation of a peptide-class II MHC complex

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; H2 DM ANTIGEN; HLA DM ANTIGEN; LYSOZYME; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PEPTIDE; PROTEIN I A KAPPA; UNCLASSIFIED DRUG;

EID: 33644550942     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.176.5.2958     Document Type: Article
Times cited : (45)

References (51)
  • 1
    • 0033301287 scopus 로고    scopus 로고
    • Structural principles of MHC class II antigen presentation
    • Nelson, C. A., and D. H. Fremont. 1999. Structural principles of MHC class II antigen presentation. Rev. Immunogenet. 1: 47-59.
    • (1999) Rev. Immunogenet. , vol.1 , pp. 47-59
    • Nelson, C.A.1    Fremont, D.H.2
  • 2
    • 0036631027 scopus 로고    scopus 로고
    • Perspective on antigen processing and presentation
    • Unanue, E. R. 2002. Perspective on antigen processing and presentation. Immunol. Rev. 185: 86-102.
    • (2002) Immunol. Rev. , vol.185 , pp. 86-102
    • Unanue, E.R.1
  • 3
    • 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., C. A. Nelson, B. Deck, and E. R. Unanue. 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
  • 4
    • 0028986855 scopus 로고
    • k-restricted determinant of hen egg lysozyme: Limitations of lymph node proliferation studies in defining immunodominance and crypticity
    • k-restricted determinant of hen egg lysozyme: limitations of lymph node proliferation studies in defining immunodominance and crypticity. Proc. Natl. Acad. Sci. USA 92: 2214-2218.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2214-2218
    • Viner, N.J.1    Nelson, C.A.2    Unanue, E.R.3
  • 5
    • 0031769696 scopus 로고    scopus 로고
    • An endogenously processed self peptide and the corresponding exogenous peptide bound to the same MHC class II molecule could be distinct ligands for TCR with different kinetic stability
    • Gyotoku, T., Y. Fukui, and T. Sasazuki. 1998. An endogenously processed self peptide and the corresponding exogenous peptide bound to the same MHC class II molecule could be distinct ligands for TCR with different kinetic stability. Eur. J. Immunol. 28: 4050-4061.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 4050-4061
    • Gyotoku, T.1    Fukui, Y.2    Sasazuki, T.3
  • 6
    • 0038302912 scopus 로고    scopus 로고
    • Altered positive selection due to corecognition of floppy peptide/MHC II conformers supports an integrative model of thymic selection
    • Viret, C., X. He, and C. A. Janeway, Jr. 2003. Altered positive selection due to corecognition of floppy peptide/MHC II conformers supports an integrative model of thymic selection. Proc. Natl. Acad. Sci. USA 100: 5354-5359.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5354-5359
    • Viret, C.1    He, X.2    Janeway Jr., C.A.3
  • 7
    • 0033548189 scopus 로고    scopus 로고
    • Conformational isomers of a class II MHC-peptide complex in solution
    • Schmitt, L., J. J. Boniface, M. M. Davis, and H. M. McConnell. 1999. Conformational isomers of a class II MHC-peptide complex in solution. J. Mol. Biol. 286: 207-218.
    • (1999) J. Mol. Biol. , vol.286 , pp. 207-218
    • Schmitt, L.1    Boniface, J.J.2    Davis, M.M.3    McConnell, H.M.4
  • 9
    • 0033213226 scopus 로고    scopus 로고
    • Quantitative analysis of the T cell repertoire that escapes negative selection
    • Peterson, D. A., R. J. DiPaolo, O. Kanagawa, and E. R. Unanue. 1999. Quantitative analysis of the T cell repertoire that escapes negative selection. Immunity 11: 453-462.
    • (1999) Immunity , vol.11 , pp. 453-462
    • Peterson, D.A.1    DiPaolo, R.J.2    Kanagawa, O.3    Unanue, E.R.4
  • 11
    • 0037173034 scopus 로고    scopus 로고
    • Distinct recognition by two subsets of T cells of an MHC class II-peptide complex
    • Pu, Z., J. A. Carrero, and E. R. Unanue. 2002. Distinct recognition by two subsets of T cells of an MHC class II-peptide complex. Proc. Natl. Acad. Sci. USA 99: 8844-8849.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8844-8849
    • Pu, Z.1    Carrero, J.A.2    Unanue, E.R.3
  • 12
    • 1842633890 scopus 로고    scopus 로고
    • T cells distinguish MHC-peptide complexes formed in separate vesicles and edited by H2-DM
    • Pu, Z., S. B. Lovitch, E. K. Bikoff, and E. R. Unanue. 2004. T cells distinguish MHC-peptide complexes formed in separate vesicles and edited by H2-DM. Immunity 20: 467-476.
    • (2004) Immunity , vol.20 , pp. 467-476
    • Pu, Z.1    Lovitch, S.B.2    Bikoff, E.K.3    Unanue, E.R.4
  • 13
    • 0028981178 scopus 로고
    • HLA-DM induces CLIP dissociation from MHC class II αβ dimers and facilitates peptide loading
    • Denzin, L. K., and P. Cresswell. 1995. HLA-DM induces CLIP dissociation from MHC class II αβ dimers and facilitates peptide loading. Cell 82: 155-165.
    • (1995) Cell , vol.82 , pp. 155-165
    • Denzin, L.K.1    Cresswell, P.2
  • 14
    • 0029084023 scopus 로고
    • DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide
    • Sherman, M. A., D. A. Weber, and P. E. Jensen. 1995. DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide. Immunity 3: 197-205.
    • (1995) Immunity , vol.3 , pp. 197-205
    • Sherman, M.A.1    Weber, D.A.2    Jensen, P.E.3
  • 16
    • 0029824101 scopus 로고    scopus 로고
    • Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM
    • Weber, D. A., B. D. Evavold, and P. E. Jensen. 1996. Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM. Science 274: 618-620.
    • (1996) Science , vol.274 , pp. 618-620
    • Weber, D.A.1    Evavold, B.D.2    Jensen, P.E.3
  • 18
    • 0029807634 scopus 로고    scopus 로고
    • Human histocompatibility leukocyte antigen (HLA)-DM edits peptides presented by HLA-DR according to their ligand binding motifs
    • van Ham, S. M., U. Gruneberg, G. Malcherek, I. Broker, A. Melms, and J. Trowsdale. 1996. Human histocompatibility leukocyte antigen (HLA)-DM edits peptides presented by HLA-DR according to their ligand binding motifs. J. Exp. Med. 184: 2019-2024.
    • (1996) J. Exp. Med. , vol.184 , pp. 2019-2024
    • Van Ham, S.M.1    Gruneberg, U.2    Malcherek, G.3    Broker, I.4    Melms, A.5    Trowsdale, J.6
  • 20
    • 0030458137 scopus 로고    scopus 로고
    • HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules
    • Denzin, L. K., C. Hammond, and P. Cresswell. 1996. HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules. J. Exp. Med. 184: 2153-2165.
    • (1996) J. Exp. Med. , vol.184 , pp. 2153-2165
    • Denzin, L.K.1    Hammond, C.2    Cresswell, P.3
  • 21
    • 0030978530 scopus 로고    scopus 로고
    • HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH
    • Kropshofer, H., S. O. Aradt, G. Moldenhauer, G. J. Hammerling, and A. B. Vogt. 1997. HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH. Immunity 6: 293-302.
    • (1997) Immunity , vol.6 , pp. 293-302
    • Kropshofer, H.1    Aradt, S.O.2    Moldenhauer, G.3    Hammerling, G.J.4    Vogt, A.B.5
  • 23
    • 0033713296 scopus 로고    scopus 로고
    • Determination of the HLA-DM interaction site on HLA-DR molecules
    • Doebele, R. C., R. Busch, H. M. Scott, A. Pashine, and E. D. Mellins. 2000. Determination of the HLA-DM interaction site on HLA-DR molecules. Immunity 13: 517-527.
    • (2000) Immunity , vol.13 , pp. 517-527
    • Doebele, R.C.1    Busch, R.2    Scott, H.M.3    Pashine, A.4    Mellins, E.D.5
  • 25
    • 0036838687 scopus 로고    scopus 로고
    • Structural factors contributing to DM susceptibility of MHC class II/peptide complexes
    • Belmares, M. P., R. Busch, K. W. Wucherpfennig, H. M. McConnell, and E. D. Mellins. 2002. Structural factors contributing to DM susceptibility of MHC class II/peptide complexes. J. Immunol. 169: 5109-5117.
    • (2002) J. Immunol. , vol.169 , pp. 5109-5117
    • Belmares, M.P.1    Busch, R.2    Wucherpfennig, K.W.3    McConnell, H.M.4    Mellins, E.D.5
  • 26
    • 0037099720 scopus 로고    scopus 로고
    • Identification of the lateral interaction surfaces of human histocompatibility leukocyte antigen (HLA)-DM with HLA-DRI by formation of tethered complexes that present enhanced HLA-DM catalysis
    • Stratikos, E., L. Mosyak, D. M. Zaller, and D. C. Wiley. 2002. Identification of the lateral interaction surfaces of human histocompatibility leukocyte antigen (HLA)-DM with HLA-DRI by formation of tethered complexes that present enhanced HLA-DM catalysis. J. Exp. Med. 196: 173-183.
    • (2002) J. Exp. Med. , vol.196 , pp. 173-183
    • Stratikos, E.1    Mosyak, L.2    Zaller, D.M.3    Wiley, D.C.4
  • 27
    • 1642495746 scopus 로고    scopus 로고
    • Enhanced catalytic action of HLA-DM on the exchange of peptides lacking backbone hydrogen bonds between their N-terminal region and the MHC class II α-chain
    • Stratikos, E., D. C. Wiley, and L. J. Stern. 2004. Enhanced catalytic action of HLA-DM on the exchange of peptides lacking backbone hydrogen bonds between their N-terminal region and the MHC class II α-chain. J. Immunol. 172: 1109-1117.
    • (2004) J. Immunol. , vol.172 , pp. 1109-1117
    • Stratikos, E.1    Wiley, D.C.2    Stern, L.J.3
  • 28
    • 0027475731 scopus 로고
    • Identification of two distinct properties of class II major histocompatibility complex-associated peptides
    • Nelson, C. A., S. J. Petzold, and E. R. Unanue. 1993. Identification of two distinct properties of class II major histocompatibility complex-associated peptides. Proc. Natl. Acad. Sci. USA 90: 1227-1231.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1227-1231
    • Nelson, C.A.1    Petzold, S.J.2    Unanue, E.R.3
  • 29
    • 0028064707 scopus 로고
    • Peptides determine the lifespan of MHC class II molecules in the antigen-presenting cell
    • Nelson, C. A., S. J. Petzold, and E. R. Unanue. 1994. Peptides determine the lifespan of MHC class II molecules in the antigen-presenting cell. Nature 371: 250-252.
    • (1994) Nature , vol.371 , pp. 250-252
    • Nelson, C.A.1    Petzold, S.J.2    Unanue, E.R.3
  • 32
    • 0018822124 scopus 로고
    • Radioiodination of proteins by the use of the chloramine-T method
    • McConahey, P. J., and F. J. Dixon. 1980. Radioiodination of proteins by the use of the chloramine-T method. Methods Enzymol. 70: 210-213.
    • (1980) Methods Enzymol. , vol.70 , pp. 210-213
    • McConahey, P.J.1    Dixon, F.J.2
  • 33
    • 0026057743 scopus 로고
    • Liposome-encapsulated antigens are processed in lysosomes, recycled, and presented to T cells
    • Harding, C. V., D. S. Collins, J. W. Slot, H. J. Geuze, and E. R. Unanue. 1991. Liposome-encapsulated antigens are processed in lysosomes, recycled, and presented to T cells. Cell 64: 393-401.
    • (1991) Cell , vol.64 , pp. 393-401
    • Harding, C.V.1    Collins, D.S.2    Slot, J.W.3    Geuze, H.J.4    Unanue, E.R.5
  • 35
    • 0000497921 scopus 로고
    • H-sensitive liposomes: Acid-induced liposome fusion
    • Connor, J., M. B. Yatvin, and L. Huang. 1984. pH-sensitive liposomes: acid-induced liposome fusion. Proc. Natl. Acad. Sci. USA 81: 1715-1718.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1715-1718
    • Connor, J.1    Yatvin, M.B.2    Huang, L.3
  • 36
    • 0026603218 scopus 로고
    • Processing of exogenous liposome-encapsulated antigens in vivo generates class I MHC-restricted T cell responses
    • Collins, D. S., K. Findlay, and C. V. Harding. 1992. Processing of exogenous liposome-encapsulated antigens in vivo generates class I MHC-restricted T cell responses. J. Immunol. 148: 3336-3341.
    • (1992) J. Immunol. , vol.148 , pp. 3336-3341
    • Collins, D.S.1    Findlay, K.2    Harding, C.V.3
  • 37
    • 0036174635 scopus 로고    scopus 로고
    • Binding interactions between peptides and proteins of the class II major histocompatibility complex
    • McFarland, B. J., and C. Beeson. 2002. Binding interactions between peptides and proteins of the class II major histocompatibility complex. Med. Res. Rev. 22: 168-203.
    • (2002) Med. Res. Rev. , vol.22 , pp. 168-203
    • McFarland, B.J.1    Beeson, C.2
  • 38
    • 0035979230 scopus 로고    scopus 로고
    • Energetic asymmetry among hydrogen bonds in MHC class II-peptide complexes
    • McFarland, B. J., J. F. Katz, C. Beeson, and A. J. Sant. 2001. Energetic asymmetry among hydrogen bonds in MHC class II-peptide complexes. Proc. Natl. Acad. Sci. USA 98: 9231-9236.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9231-9236
    • McFarland, B.J.1    Katz, J.F.2    Beeson, C.3    Sant, A.J.4
  • 39
    • 0031744254 scopus 로고    scopus 로고
    • Alteration of a single hydrogen bond between class II molecules and peptide results in rapid degradation of class II molecules after invariant chain removal
    • Ceman, S., S. Wu, T. S. Jardetzky, and A. J. Sant. 1998. Alteration of a single hydrogen bond between class II molecules and peptide results in rapid degradation of class II molecules after invariant chain removal. J. Exp. Med. 188: 2139-2149.
    • (1998) J. Exp. Med. , vol.188 , pp. 2139-2149
    • Ceman, S.1    Wu, S.2    Jardetzky, T.S.3    Sant, A.J.4
  • 40
    • 0033214398 scopus 로고    scopus 로고
    • Cutting edge: A single, essential hydrogen bond controls the stability of peptide-MHC class II complexes
    • McFarland, B. J., C. Beeson, and A. J. Sant. 1999. Cutting edge: a single, essential hydrogen bond controls the stability of peptide-MHC class II complexes. J. Immunol 163: 3567-3571.
    • (1999) J. Immunol , vol.163 , pp. 3567-3571
    • McFarland, B.J.1    Beeson, C.2    Sant, A.J.3
  • 41
    • 0035892901 scopus 로고    scopus 로고
    • Hydrogen bond integrity between MHC class II molecules and bound peptide determines the intracellular fate of MHC class II molecules
    • Arneson, L. S., J. F. Katz, M. Liu, and A. J. Sant. 2001. Hydrogen bond integrity between MHC class II molecules and bound peptide determines the intracellular fate of MHC class II molecules. J. Immunol. 167: 6939-6946.
    • (2001) J. Immunol. , vol.167 , pp. 6939-6946
    • Arneson, L.S.1    Katz, J.F.2    Liu, M.3    Sant, A.J.4
  • 42
    • 0034995149 scopus 로고    scopus 로고
    • Mutations changing the kinetics of class II MHC peptide exchange
    • Wilson, N., D. Fremont, P. Marrack, and J. Kappler. 2001. Mutations changing the kinetics of class II MHC peptide exchange. Immunity 5: 513-522.
    • (2001) Immunity , vol.5 , pp. 513-522
    • Wilson, N.1    Fremont, D.2    Marrack, P.3    Kappler, J.4
  • 43
    • 0037169536 scopus 로고    scopus 로고
    • Ligand exchange of major histocompatibility complex class II proteins is triggered by H-bond donor groups of small molecules
    • Falk, K., J. M. Lau, L. Santambrogio, V. M. Esteban, F. Puentes, O. Rotzschke, and J. L. Strominger. 2002. Ligand exchange of major histocompatibility complex class II proteins is triggered by H-bond donor groups of small molecules. J. Biol. Chem. 277: 2709-2715.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2709-2715
    • Falk, K.1    Lau, J.M.2    Santambrogio, L.3    Esteban, V.M.4    Puentes, F.5    Rotzschke, O.6    Strominger, J.L.7
  • 44
    • 10944263783 scopus 로고    scopus 로고
    • Chemical analogues" of HLA-DM can induce a peptide-receptive state in HLA-DR molecules
    • Marin-Esteban, V., K. Falk, and O. Rotzschke. 2004. "Chemical analogues" of HLA-DM can induce a peptide-receptive state in HLA-DR molecules. J. Biol. Chem. 279: 50684-50690.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50684-50690
    • Marin-Esteban, V.1    Falk, K.2    Rotzschke, O.3
  • 45
    • 0033615531 scopus 로고    scopus 로고
    • Two structural states of complexes of peptide and class II major histocompatibility complex revealed by photoaffinity-labeled peptides
    • Carrasco-Marin, E., S. Petzold, and E. R. Unanue. 1999. Two structural states of complexes of peptide and class II major histocompatibility complex revealed by photoaffinity-labeled peptides. J. Biol. Chem. 274: 31333-31340.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31333-31340
    • Carrasco-Marin, E.1    Petzold, S.2    Unanue, E.R.3
  • 46
    • 0029055938 scopus 로고
    • Antigen presentation mediated by recycling of surface HLA-DR molecules
    • Pinet, V., M. Vergelli, R. Martin, O. Bakke, and E. O. Long. 1995. Antigen presentation mediated by recycling of surface HLA-DR molecules. Nature 375: 603-606.
    • (1995) Nature , vol.375 , pp. 603-606
    • Pinet, V.1    Vergelli, M.2    Martin, R.3    Bakke, O.4    Long, E.O.5
  • 47
    • 0030451002 scopus 로고    scopus 로고
    • Distinct antigen-MHC class II complexes generated by separate processing pathways
    • Lindner, R., and E. R. Unanue. 1996. Distinct antigen-MHC class II complexes generated by separate processing pathways. EMBO J. 15: 6910-6920.
    • (1996) EMBO J. , vol.15 , pp. 6910-6920
    • Lindner, R.1    Unanue, E.R.2
  • 48
    • 0031568395 scopus 로고    scopus 로고
    • Early endosomes and a late endocytic compartment generate different peptide-class II MHC complexes via distinct processing mechanisms
    • Griffin, J. P., R. Chu, and C. V. Harding. 1997. Early endosomes and a late endocytic compartment generate different peptide-class II MHC complexes via distinct processing mechanisms. J. Immunol. 158: 1523-1532.
    • (1997) J. Immunol. , vol.158 , pp. 1523-1532
    • Griffin, J.P.1    Chu, R.2    Harding, C.V.3
  • 50
    • 0035451091 scopus 로고    scopus 로고
    • Neutrophils process exogenous bacteria via an alternate class I MHC processing pathway for presentation of peptides to T lymphocytes
    • Potter, N. S., and C. V. Harding. 2001. Neutrophils process exogenous bacteria via an alternate class I MHC processing pathway for presentation of peptides to T lymphocytes. J. Immunol. 167: 2538-2546.
    • (2001) J. Immunol. , vol.167 , pp. 2538-2546
    • Potter, N.S.1    Harding, C.V.2
  • 51
    • 0031030323 scopus 로고    scopus 로고
    • Amino-terminal trimming of peptides for presentation on major histocompatibility complex class II molecules
    • Nelson, C. A., I. Vidavsky, N. J. Viner, M. L. Gross, and E. R. Unanue. 1997. Amino-terminal trimming of peptides for presentation on major histocompatibility complex class II molecules. Proc. Natl. Acad. Sci. USA 94: 628-633.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 628-633
    • Nelson, C.A.1    Vidavsky, I.2    Viner, N.J.3    Gross, M.L.4    Unanue, E.R.5


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