메뉴 건너뛰기




Volumn 47, Issue 1-3, 2010, Pages 56-64

Conformational heterogeneity of MHC class II induced upon binding to different peptides is a key regulator in antigen presentation and epitope selection

Author keywords

Conformational heterogeneity; H bonds; Immunodominance; Kinetics; MHC class II; Peptide receptive conformation

Indexed keywords

ALPHA ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR; CHAPERONE; EPITOPE; HETERODIMER; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; TAPASIN; HLA ANTIGEN CLASS 2; HLA D ANTIGEN; HLA-DM ANTIGENS; PEPTIDE;

EID: 77953960092     PISSN: 0257277X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12026-009-8138-1     Document Type: Review
Times cited : (22)

References (47)
  • 1
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • 10.1146/annurev.iy.11.040193.002155 8476568
    • RN Germain DH Margulies 1993 The biochemistry and cell biology of antigen processing and presentation Annu Rev Immunol 11 403 450 10.1146/annurev.iy.11. 040193.002155 8476568
    • (1993) Annu Rev Immunol , vol.11 , pp. 403-450
    • Germain, R.N.1    Margulies, D.H.2
  • 2
    • 0026584496 scopus 로고
    • How MHC class II molecules work: Peptide-dependent completion of protein folding
    • 10.1016/0167-5699(92)90131-P 1533524
    • S Sadegh-Nasseri RN Germain 1992 How MHC class II molecules work: peptide-dependent completion of protein folding Immunol Today 13 2 43 46 10.1016/0167-5699(92)90131-P 1533524
    • (1992) Immunol Today , vol.13 , Issue.2 , pp. 43-46
    • Sadegh-Nasseri, S.1    Germain, R.N.2
  • 3
    • 0025870669 scopus 로고
    • A role for peptide in determining MHC class II structure
    • 10.1038/353167a0 1653903
    • S Sadegh-Nasseri RN Germain 1991 A role for peptide in determining MHC class II structure Nature 353 6340 167 170 10.1038/353167a0 1653903
    • (1991) Nature , vol.353 , Issue.6340 , pp. 167-170
    • Sadegh-Nasseri, S.1    Germain, R.N.2
  • 4
    • 0024501330 scopus 로고
    • A kinetic intermediate in the reaction of an antigenic peptide and I-E(k)
    • DOI 10.1038/337274a0
    • S Sadegh-Nasseri HM McConnell 1989 A kinetic intermediate in the reaction of an antigenic peptide and I-Ek Nature 337 6204 274 276 10.1038/337274a0 2536141 (Pubitemid 19030566)
    • (1989) Nature , vol.337 , Issue.6204 , pp. 274-276
    • Sadegh-Nasseri, S.1    McConnell, H.M.2
  • 5
    • 0027941809 scopus 로고
    • MHC class II function preserved by low-affinity peptide interactions preceding stable binding
    • DOI 10.1038/370647a0
    • S Sadegh-Nasseri LJ Stern DC Wiley RN Germain 1994 MHC class II function preserved by low-affinity peptide interactions preceding stable binding Nature 370 6491 647 650 10.1038/370647a0 8065450 (Pubitemid 24270684)
    • (1994) Nature , vol.370 , Issue.6491 , pp. 647-650
    • Sadegh-Nasseri, S.1    Stern, L.J.2    Wiley, D.C.3    Germain, R.N.4
  • 7
    • 27144451208 scopus 로고    scopus 로고
    • Probing the ligand-induced conformational change in HLA-DR1 by selective chemical modification and mass spectrometric mapping
    • DOI 10.1021/bi050972p
    • GJ Carven LJ Stern 2005 Probing the ligand-induced conformational change in HLA-DR1 by selective chemical modification and mass spectrometric mapping Biochemistry 44 42 13625 13637 10.1021/bi050972p 16229453 (Pubitemid 41507444)
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 13625-13637
    • Carven, G.J.1    Stern, L.J.2
  • 8
    • 0024953878 scopus 로고
    • Structural intermediates in the reactions of antigenic peptides with MHC molecules
    • 2639762
    • K Dornmair B Rothenhausler HM McConnell 1989 Structural intermediates in the reactions of antigenic peptides with MHC molecules Cold Spring Harb Symp Quant Biol 54 Pt 1 409 416 2639762
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PART 1 , pp. 409-416
    • Dornmair, K.1    Rothenhausler, B.2    McConnell, H.M.3
  • 9
    • 0028213924 scopus 로고
    • Formation and dissociation of short-lived class II MHC-peptide complexes
    • 10.1021/bi00173a032 8110789
    • SN Witt HM McConnell 1994 Formation and dissociation of short-lived class II MHC-peptide complexes Biochemistry 33 7 1861 1868 10.1021/bi00173a032 8110789
    • (1994) Biochemistry , vol.33 , Issue.7 , pp. 1861-1868
    • Witt, S.N.1    McConnell, H.M.2
  • 10
    • 0033548189 scopus 로고    scopus 로고
    • Conformational isomers of a class II MHC-peptide complex in solution
    • DOI 10.1006/jmbi.1998.2463
    • L Schmitt JJ Boniface MM Davis HM McConnell 1999 Conformational isomers of a class II MHC-peptide complex in solution J Mol Biol 286 1 207 218 10.1006/jmbi.1998.2463 9931260 (Pubitemid 29078406)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.1 , pp. 207-218
    • Schmitt, L.1    Boniface, J.J.2    Davis, M.M.3    McConnell, H.M.4
  • 11
    • 0033120523 scopus 로고    scopus 로고
    • Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides
    • 10201925
    • SK Natarajan M Assadi S Sadegh-Nasseri 1999 Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides J Immunol 162 7 4030 4036 10201925
    • (1999) J Immunol , vol.162 , Issue.7 , pp. 4030-4036
    • Natarajan, S.K.1    Assadi, M.2    Sadegh-Nasseri, S.3
  • 15
    • 0022894853 scopus 로고
    • Isolation and characterization of antigen-IA complexes involved in T cell recognition
    • 10.1016/0092-8674(86)90822-6 3490919
    • S Buus A Sette SM Colon DM Jenis HM Grey 1986 Isolation and characterization of antigen-IA complexes involved in T cell recognition Cell 47 6 1071 1077 10.1016/0092-8674(86)90822-6 3490919
    • (1986) Cell , vol.47 , Issue.6 , pp. 1071-1077
    • Buus, S.1    Sette, A.2    Colon, S.M.3    Jenis, D.M.4    Grey, H.M.5
  • 16
    • 0025358699 scopus 로고
    • Refolding and reassembly of separate α and β chains of class II molecules of the major histocompatibility complex leads to increased peptide-binding capacity
    • DOI 10.1073/pnas.87.11.4134
    • K Dornmair HM McConnell 1990 Refolding and reassembly of separate alpha and beta chains of class II molecules of the major histocompatibility complex leads to increased peptide-binding capacity Proc Natl Acad Sci USA 87 11 4134 4138 10.1073/pnas.87.11.4134 2349223 (Pubitemid 20217996)
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , Issue.11 , pp. 4134-4138
    • Dornmair, K.1    McConnell, H.M.2
  • 17
    • 0025826118 scopus 로고
    • MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding
    • 10.1038/353134a0 1891045
    • RN Germain LR Hendrix 1991 MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding Nature 353 6340 134 139 10.1038/353134a0 1891045
    • (1991) Nature , vol.353 , Issue.6340 , pp. 134-139
    • Germain, R.N.1    Hendrix, L.R.2
  • 18
    • 0025939316 scopus 로고
    • Processed antigen binds to newly synthesized MHC class II molecules in antigen-specific b lymphocytes
    • 10.1016/0092-8674(91)90575-J 1913812
    • HW Davidson PA Reid A Lanzavecchia C Watts 1991 Processed antigen binds to newly synthesized MHC class II molecules in antigen-specific b lymphocytes Cell 67 1 105 116 10.1016/0092-8674(91)90575-J 1913812
    • (1991) Cell , vol.67 , Issue.1 , pp. 105-116
    • Davidson, H.W.1    Reid, P.A.2    Lanzavecchia, A.3    Watts, C.4
  • 19
    • 2142774531 scopus 로고
    • Peptide, invariant chain, or molecular aggregation preserves class II from functional inactivation
    • R.E. Humphreys S.K. Pierce (eds). Academic Press San Diego
    • Sadegh-Nasseri S. Peptide, invariant chain, or molecular aggregation preserves class II from functional inactivation. In: Humphreys RE, Pierce SK, editors. Antigen processing and presentation, vol. 1. San Diego: Academic Press; 1994. p. 170-87.
    • (1994) Antigen Processing and Presentation 1 , pp. 170-187
    • Sadegh-Nasseri, S.1
  • 20
    • 0028791680 scopus 로고
    • Invariant chain made in Escherichia coli has an exposed n-terminal segment that blocks antigen binding to HLA-DR1 and a trimeric c-terminal segment that binds empty HLA-DR1
    • 10.1073/pnas.92.24.11289 7479981
    • SJ Park S Sadegh-Nasseri DC Wiley 1995 Invariant chain made in Escherichia coli has an exposed n-terminal segment that blocks antigen binding to HLA-DR1 and a trimeric c-terminal segment that binds empty HLA-DR1 Proc Natl Acad Sci USA 92 24 11289 11293 10.1073/pnas.92.24.11289 7479981
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.24 , pp. 11289-11293
    • Park, S.J.1    Sadegh-Nasseri, S.2    Wiley, D.C.3
  • 21
    • 0025369192 scopus 로고
    • Peptide binding to HLA-DR1: A peptide with most residues substituted to alanine retains MHC binding
    • 2189723
    • TS Jardetzky JC Gorga R Busch J Rothbard JL Strominger DC Wiley 1990 Peptide binding to HLA-DR1: a peptide with most residues substituted to alanine retains MHC binding EMBO J 9 6 1797 1803 2189723
    • (1990) EMBO J , vol.9 , Issue.6 , pp. 1797-1803
    • Jardetzky, T.S.1    Gorga, J.C.2    Busch, R.3    Rothbard, J.4    Strominger, J.L.5    Wiley, D.C.6
  • 22
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • DOI 10.1038/368215a0
    • LJ Stern JH Brown TS Jardetzky JC Gorga RG Urban JL Strominger DC Wiley 1994 Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide Nature 368 6468 215 221 10.1038/368215a0 8145819 (Pubitemid 24108837)
    • (1994) Nature , vol.368 , Issue.6468 , pp. 215-221
    • 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
  • 23
    • 0031572833 scopus 로고    scopus 로고
    • The class II MHC protein HLA-DR1 in complex with an endogenous peptide: Implications for the structural basis of the specificity of peptide binding
    • 10.1016/S0969-2126(97)00288-8 9351812
    • VL Murthy LJ Stern 1997 The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding Structure 5 10 1385 1396 10.1016/S0969-2126(97)00288-8 9351812
    • (1997) Structure , vol.5 , Issue.10 , pp. 1385-1396
    • Murthy, V.L.1    Stern, L.J.2
  • 24
    • 0027185153 scopus 로고
    • Promiscuous and allele-specific anchors in HLA-DR-binding peptides
    • DOI 10.1016/0092-8674(93)90306-B
    • J Hammer P Valsasnini K Tolba D Bolin J Higelin B Takacs F Sinigaglia 1993 Promiscuous and allele-specific anchors in HLA-DR-binding peptides Cell 74 1 197 203 10.1016/0092-8674(93)90306-B 8334703 (Pubitemid 23219890)
    • (1993) Cell , vol.74 , Issue.1 , pp. 197-203
    • Hammer, J.1    Valsasnini, P.2    Tolba, K.3    Bolin, D.4    Higelin, J.5    Takacs, B.6    Sinigaglia, F.7
  • 25
    • 0029963942 scopus 로고    scopus 로고
    • T cell recognition of MHC class II-associated peptides is independent of peptide affinity for MHC and sodium dodecyl sulfate stability of the peptide/MHC complex. Effects of conservative amino acid substitutions at anchor position 1 of influenza matrix protein19-31
    • 8621918
    • S Wu J Gorski DD Eckels DK Newton-Nash 1996 T cell recognition of MHC class II-associated peptides is independent of peptide affinity for MHC and sodium dodecyl sulfate stability of the peptide/MHC complex. Effects of conservative amino acid substitutions at anchor position 1 of influenza matrix protein19-31 J Immunol 156 10 3815 3820 8621918
    • (1996) J Immunol , vol.156 , Issue.10 , pp. 3815-3820
    • Wu, S.1    Gorski, J.2    Eckels, D.D.3    Newton-Nash, D.K.4
  • 27
    • 0026733449 scopus 로고
    • Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size
    • 10.1038/358764a0 1380674
    • RM Chicz RG Urban WS Lane JC Gorga LJ Stern DA Vignali JL Strominger 1992 Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size Nature 358 6389 764 768 10.1038/358764a0 1380674
    • (1992) Nature , vol.358 , Issue.6389 , pp. 764-768
    • Chicz, R.M.1    Urban, R.G.2    Lane, W.S.3    Gorga, J.C.4    Stern, L.J.5    Vignali, D.A.6    Strominger, J.L.7
  • 28
    • 0033559513 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate stability of HLA-DR1 complexes correlates with burial of hydrophobic residues in pocket 1
    • 10092802
    • SK Natarajan LJ Stern S Sadegh-Nasseri 1999 Sodium dodecyl sulfate stability of HLA-DR1 complexes correlates with burial of hydrophobic residues in pocket 1 J Immunol 162 6 3463 3470 10092802
    • (1999) J Immunol , vol.162 , Issue.6 , pp. 3463-3470
    • Natarajan, S.K.1    Stern, L.J.2    Sadegh-Nasseri, S.3
  • 29
    • 0026571278 scopus 로고
    • The human class II MHC protein HLA-DR1 assembles as empty alpha beta heterodimers in the absence of antigenic peptide
    • 10.1016/0092-8674(92)90184-E 1371238
    • LJ Stern DC Wiley 1992 The human class II MHC protein HLA-DR1 assembles as empty alpha beta heterodimers in the absence of antigenic peptide Cell 68 3 465 477 10.1016/0092-8674(92)90184-E 1371238
    • (1992) Cell , vol.68 , Issue.3 , pp. 465-477
    • Stern, L.J.1    Wiley, D.C.2
  • 30
    • 0027303736 scopus 로고
    • Peptide binding inhibits protein aggregation of invariant-chain free class II dimers and promotes surface expression of occupied molecules
    • DOI 10.1038/363725a0
    • RN Germain AG Rinker Jr 1993 Peptide binding inhibits protein aggregation of invariant-chain free class II dimers and promotes surface expression of occupied molecules Nature 363 6431 725 728 10.1038/363725a0 8515815 (Pubitemid 23227650)
    • (1993) Nature , vol.363 , Issue.6431 , pp. 725-728
    • Germaln, R.N.1    Rinker Jr., A.G.2
  • 31
    • 0028136262 scopus 로고
    • The CLIP region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding, transport, and peptide occupancy
    • DOI 10.1084/jem.180.3.1107
    • P Romagnoli RN Germain 1994 The clip region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding, transport, and peptide occupancy J Exp Med 180 3 1107 1113 10.1084/jem.180.3. 1107 8064228 (Pubitemid 24256623)
    • (1994) Journal of Experimental Medicine , vol.180 , Issue.3 , pp. 1107-1113
    • Romagnoli, P.1    Germain, R.N.2
  • 32
    • 0034684671 scopus 로고    scopus 로고
    • HLA-DM recognizes the flexible conformation of major histocompatibility complex class II
    • DOI 10.1084/jem.192.12.1697
    • CL Chou S Sadegh-Nasseri 2000 HLA-dm recognizes the flexible conformation of major histocompatibility complex class II J Exp Med 192 12 1697 1706 10.1084/jem.192.12.1697 11120767 (Pubitemid 32049763)
    • (2000) Journal of Experimental Medicine , vol.192 , Issue.12 , pp. 1697-1706
    • Chou, C.-L.1    Sadegh-Nasseri, S.2
  • 33
    • 1842633890 scopus 로고    scopus 로고
    • T cells distinguish MHC-peptide complexes formed in separate vesicles and edited by H2-DM
    • DOI 10.1016/S1074-7613(04)00073-1, PII S1074761304000731
    • Z Pu SB Lovitch EK Bikoff ER Unanue 2004 T cells distinguish MHC-peptide complexes formed in separate vesicles and edited by H2-DM Immunity 20 4 467 476 10.1016/S1074-7613(04)00073-1 15084275 (Pubitemid 38482124)
    • (2004) Immunity , vol.20 , Issue.4 , pp. 467-476
    • Pu, Z.1    Lovitch, S.B.2    Bikoff, E.K.3    Unanue, E.R.4
  • 34
    • 10944263783 scopus 로고    scopus 로고
    • "Chemical analogues" of HLA-DM can induce a peptide-receptive state in HLA-DR molecules
    • DOI 10.1074/jbc.M407598200
    • V Marin-Esteban K Falk O Rotzschke 2004 "Chemical analogues" Of HLA-DM can induce a peptide-receptive state in HLA-DR molecules J Biol Chem 279 49 50684 50690 10.1074/jbc.M407598200 15381703 (Pubitemid 40017805)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50684-50690
    • Marin-Esteban, V.1    Falk, K.2    Rotzschke, O.3
  • 35
    • 0041429632 scopus 로고    scopus 로고
    • Interaction of HLA-DR with an acidic face of HLA-DM disrupts sequence-dependent interactions with peptides
    • DOI 10.1016/S1074-7613(03)00200-0
    • A Pashine R Busch MP Belmares JN Munning RC Doebele M Buckingham GP Nolan ED Mellins 2003 Interaction of HLA-DR with an acidic face of HLA-DM disrupts sequence-dependent interactions with peptides Immunity 19 2 183 192 10.1016/S1074-7613(03)00200-0 12932352 (Pubitemid 37011333)
    • (2003) Immunity , vol.19 , Issue.2 , pp. 183-192
    • Pashine, A.1    Busch, R.2    Belmares, M.P.3    Munning, J.N.4    Doebele, R.C.5    Buckingham, M.6    Nolan, G.P.7    Mellins, E.D.8
  • 36
    • 0347926117 scopus 로고    scopus 로고
    • Formation of two peptide/MHC II isomers is catalyzed differentially by HLA-DM
    • DOI 10.1021/bi020466p
    • MP Belmares R Busch ED Mellins HM McConnell 2003 Formation of two peptide/MHC II isomers is catalyzed differentially by HLA-DM Biochemistry 42 3 838 847 10.1021/bi020466p 12534297 (Pubitemid 36133309)
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 838-847
    • Belmares, M.P.1    Busch, R.2    Mellins, E.D.3    McConnell, H.M.4
  • 37
    • 0037099720 scopus 로고    scopus 로고
    • Identification of the lateral interaction surfaces of human histocompatibility leukocyte antigen (HLA)-DM with HLA-DR1 by formation of tethered complexes that present enhanced HLA-DM catalysis
    • DOI 10.1084/jem.20020117
    • E Stratikos L Mosyak DM Zaller DC Wiley 2002 Identification of the lateral interaction surfaces of human histocompatibility leukocyte antigen (HLA)-DM with HLA-DR1 by formation of tethered complexes that present enhanced HLA-dm catalysis J Exp Med 196 2 173 183 10.1084/jem.20020117 12119342 (Pubitemid 34787507)
    • (2002) Journal of Experimental Medicine , vol.196 , Issue.2 , pp. 173-183
    • Stratikos, E.1    Mosyak, L.2    Zaller, D.M.3    Wiley, D.C.4
  • 38
    • 0033713296 scopus 로고    scopus 로고
    • Determination of the HLA-DM interaction site on HLA-DR molecules
    • 10.1016/S1074-7613(00)00051-0 11070170
    • RC Doebele R Busch HM Scott A Pashine ED Mellins 2000 Determination of the HLA-DM interaction site on HLA-DR molecules Immunity 13 4 517 527 10.1016/S1074-7613(00)00051-0 11070170
    • (2000) Immunity , vol.13 , Issue.4 , pp. 517-527
    • Doebele, R.C.1    Busch, R.2    Scott, H.M.3    Pashine, A.4    Mellins, E.D.5
  • 39
    • 33846952190 scopus 로고    scopus 로고
    • HLA-DM targets the hydrogen bond between the histidine at position β81 and peptide to dissociate HLA-DR-peptide complexes
    • DOI 10.1038/ni1414, PII NI1414
    • K Narayan CL Chou A Kim IZ Hartman S Dalai S Khoruzhenko S Sadegh-Nasseri 2007 HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes Nat Immunol 8 1 92 100 10.1038/ni1414 17143275 (Pubitemid 46242363)
    • (2007) Nature Immunology , vol.8 , Issue.1 , pp. 92-100
    • Narayan, K.1    Chou, C.-L.2    Kim, A.3    Hartman, I.Z.4    Dalai, S.5    Khoruzhenko, S.6    Sadegh-Nasseri, S.7
  • 40
    • 0029782111 scopus 로고    scopus 로고
    • Structures of an MHC class II molecule with covalently bound single peptides
    • 10.1126/science.272.5264.1001 8638119
    • DH Fremont WA HenDRickson P Marrack J Kappler 1996 Structures of an MHC class II molecule with covalently bound single peptides Science 272 5264 1001 1004 10.1126/science.272.5264.1001 8638119
    • (1996) Science , vol.272 , Issue.5264 , pp. 1001-1004
    • Fremont, D.H.1    Hendrickson, W.A.2    Marrack, P.3    Kappler, J.4
  • 41
    • 0032033445 scopus 로고    scopus 로고
    • Crystal structure of I-A(k) in complex with a dominant epitope of lysozyme
    • DOI 10.1016/S1074-7613(00)80536-1
    • DH Fremont D Monnaie CA Nelson WA HenDRickson ER Unanue 1998 Crystal structure of I-Ak in complex with a dominant epitope of lysozyme Immunity 8 3 305 317 10.1016/S1074-7613(00)80536-1 9529148 (Pubitemid 28188891)
    • (1998) Immunity , vol.8 , Issue.3 , pp. 305-317
    • Fremont, D.H.1    Monnaie, D.2    Nelson, C.A.3    Hendrickson, W.A.4    Unanue, E.R.5
  • 42
    • 0034995149 scopus 로고    scopus 로고
    • Mutations changing the kinetics of class II MHC peptide exchange
    • DOI 10.1016/S1074-7613(01)00140-6
    • N Wilson D Fremont P Marrack J Kappler 2001 Mutations changing the kinetics of class II MHC peptide exchange Immunity 14 5 513 522 10.1016/S1074-7613(01)00140-6 11371354 (Pubitemid 32520863)
    • (2001) Immunity , vol.14 , Issue.5 , pp. 513-522
    • Wilson, N.1    Fremont, D.2    Marrack, P.3    Kappler, J.4
  • 43
    • 0033214398 scopus 로고    scopus 로고
    • Cutting edge: A single, essential hydrogen bond controls the stability of peptide-MHC class II complexes
    • 10490947
    • BJ McFarland C Beeson AJ Sant 1999 Cutting edge: a single, essential hydrogen bond controls the stability of peptide-MHC class II complexes J Immunol 163 7 3567 3571 10490947
    • (1999) J Immunol , vol.163 , Issue.7 , pp. 3567-3571
    • McFarland, B.J.1    Beeson, C.2    Sant, A.J.3
  • 44
    • 0942286863 scopus 로고    scopus 로고
    • Contribution of a single hydrogen bond between betahis81 of MHC class II I-E(k) and the bound peptide to the PH-dependent thermal stability
    • 14734858
    • K Saito M Oda A Sarai T Azuma H Kozono 2004 Contribution of a single hydrogen bond between betahis81 of MHC class II I-E(k) and the bound peptide to the PH-dependent thermal stability Microbiol Immunol 48 1 53 57 14734858
    • (2004) Microbiol Immunol , vol.48 , Issue.1 , pp. 53-57
    • Saito, K.1    Oda, M.2    Sarai, A.3    Azuma, T.4    Kozono, H.5
  • 45
    • 39749142543 scopus 로고    scopus 로고
    • The convergent roles of tapasin and HLA-DM in antigen presentation
    • 10.1016/j.it.2008.01.001 18261958
    • S Sadegh-Nasseri M Chen K Narayan M Bouvier 2008 The convergent roles of tapasin and HLA-DM in antigen presentation Trends Immunol 29 3 141 147 10.1016/j.it.2008.01.001 18261958
    • (2008) Trends Immunol , vol.29 , Issue.3 , pp. 141-147
    • Sadegh-Nasseri, S.1    Chen, M.2    Narayan, K.3    Bouvier, M.4
  • 46
    • 68749117718 scopus 로고    scopus 로고
    • HLA-DM mediates peptide exchange by interacting transiently and repeatedly with HLA-DR1
    • 10.1016/j.molimm.2009.07.001 19647320
    • K Narayan KW Su CL Chou S Khoruzhenko S Sadegh-Nasseri 2009 HLA-DM mediates peptide exchange by interacting transiently and repeatedly with HLA-DR1 Mol Immunol 46 15 3157 3162 10.1016/j.molimm.2009.07.001 19647320
    • (2009) Mol Immunol , vol.46 , Issue.15 , pp. 3157-3162
    • Narayan, K.1    Su, K.W.2    Chou, C.L.3    Khoruzhenko, S.4    Sadegh-Nasseri, S.5
  • 47
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • DOI 10.1038/sj.emboj.7601624, PII 7601624
    • M Chen M Bouvier 2007 Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection EMBO J 26 6 1681 1690 10.1038/sj.emboj.7601624 17332746 (Pubitemid 46480944)
    • (2007) EMBO Journal , vol.26 , Issue.6 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.