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Volumn 250, Issue 1, 2012, Pages 10-31

Structural and dynamic control of T-cell receptor specificity, cross-reactivity, and binding mechanism

Author keywords

Cross reactivity; MHC; Molecular flexibility; Specificity; Structure; T cell receptor

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN; MELAN A; MELANOMA VACCINE; PEPTIDE VACCINE; T LYMPHOCYTE RECEPTOR;

EID: 84867426149     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/j.1600-065X.2012.01165.x     Document Type: Article
Times cited : (71)

References (134)
  • 1
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern LJ, et al. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 1994;368:215-221.
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.J.1
  • 3
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 1996;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
  • 4
    • 0029662223 scopus 로고    scopus 로고
    • An alphabeta T cell receptor structure at 2.5 A and its orientation in the TCR-MHC complex
    • Garcia KC, et al. An alphabeta T cell receptor structure at 2.5 A and its orientation in the TCR-MHC complex. Science 1996;274:209-219.
    • (1996) Science , vol.274 , pp. 209-219
    • Garcia, K.C.1
  • 5
    • 0016318314 scopus 로고
    • Immunological surveillance against altered self components by sensitised T lymphocytes in lymphocytes choriomeningitis
    • Zinkernagel RM, Doherty PC. Immunological surveillance against altered self components by sensitised T lymphocytes in lymphocytes choriomeningitis. Nature 1974;251:547-548.
    • (1974) Nature , vol.251 , pp. 547-548
    • Zinkernagel, R.M.1    Doherty, P.C.2
  • 6
    • 0031868554 scopus 로고    scopus 로고
    • Anatomy of an antibody molecule: structure, kinetics, thermodynamics and mutational studies of the antilysozyme antibody D1.3
    • Braden BC, Goldman ER, Mariuzza RA, Poljak RJ. Anatomy of an antibody molecule: structure, kinetics, thermodynamics and mutational studies of the antilysozyme antibody D1.3. Immunol Rev 1998;163:45-57.
    • (1998) Immunol Rev , vol.163 , pp. 45-57
    • Braden, B.C.1    Goldman, E.R.2    Mariuzza, R.A.3    Poljak, R.J.4
  • 8
    • 0032171644 scopus 로고    scopus 로고
    • A very high level of crossreactivity is an essential feature of the T-cell receptor
    • Mason D. A very high level of crossreactivity is an essential feature of the T-cell receptor. Immunol Today 1998;19:395-404.
    • (1998) Immunol Today , vol.19 , pp. 395-404
    • Mason, D.1
  • 9
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia KC, et al. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 1998;279:1166-1172.
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1
  • 10
    • 0030033451 scopus 로고    scopus 로고
    • Analysis of the T-cell receptor repertoire of human T-cell leukemia virus type 1 (HTLV-1) Tax-specific CD8+ cytotoxic T lymphocytes from patients with HTLV-1-associated disease: evidence for oligoclonal expansion
    • Utz U, Banks D, Jacobson S, Biddison WE. Analysis of the T-cell receptor repertoire of human T-cell leukemia virus type 1 (HTLV-1) Tax-specific CD8+ cytotoxic T lymphocytes from patients with HTLV-1-associated disease: evidence for oligoclonal expansion. J Virol 1996;70:843-851.
    • (1996) J Virol , vol.70 , pp. 843-851
    • Utz, U.1    Banks, D.2    Jacobson, S.3    Biddison, W.E.4
  • 11
    • 0033136726 scopus 로고    scopus 로고
    • Peptide recognition by two HLA-A2/Ta11-19-specific T cell clones in relationship to their MHC/peptide/TCR crystal structures
    • Hausmann S, et al. Peptide recognition by two HLA-A2/Ta11-19-specific T cell clones in relationship to their MHC/peptide/TCR crystal structures. J Immunol 1999;162:5389-5397.
    • (1999) J Immunol , vol.162 , pp. 5389-5397
    • Hausmann, S.1
  • 12
    • 0033165928 scopus 로고    scopus 로고
    • Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
    • Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC. Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity 1999;11:45-56.
    • (1999) Immunity , vol.11 , pp. 45-56
    • Ding, Y.H.1    Baker, B.M.2    Garboczi, D.N.3    Biddison, W.E.4    Wiley, D.C.5
  • 13
    • 0033711639 scopus 로고    scopus 로고
    • Conversion of a T cell antagonist into an agonist by repairing a defect in the TCR/Peptide/MHC interface. Implications for TCR Signaling
    • Baker BM, Gagnon SJ, Biddison WE, Wiley DC. Conversion of a T cell antagonist into an agonist by repairing a defect in the TCR/Peptide/MHC interface. Implications for TCR Signaling. Immunity 2000;13:475-484.
    • (2000) Immunity , vol.13 , pp. 475-484
    • Baker, B.M.1    Gagnon, S.J.2    Biddison, W.E.3    Wiley, D.C.4
  • 14
    • 34247346627 scopus 로고    scopus 로고
    • How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?
    • Mazza C, et al. How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides? EMBO J 2007;26:1972-1983.
    • (2007) EMBO J , vol.26 , pp. 1972-1983
    • Mazza, C.1
  • 15
    • 18344394144 scopus 로고    scopus 로고
    • A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex
    • Reiser JB, et al. A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. Immunity 2002;16:345-354.
    • (2002) Immunity , vol.16 , pp. 345-354
    • Reiser, J.B.1
  • 16
    • 0037342030 scopus 로고    scopus 로고
    • CDR3 loop flexibility contributes to the degeneracy of TCR recognition
    • Reiser JB, et al. CDR3 loop flexibility contributes to the degeneracy of TCR recognition. Nat Immunol 2003;4:241-247.
    • (2003) Nat Immunol , vol.4 , pp. 241-247
    • Reiser, J.B.1
  • 17
    • 34247154800 scopus 로고    scopus 로고
    • A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule
    • Tynan FE, et al. A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Nat Immunol 2007;8:268-276.
    • (2007) Nat Immunol , vol.8 , pp. 268-276
    • Tynan, F.E.1
  • 18
    • 20944450033 scopus 로고    scopus 로고
    • Structural and kinetic basis for heightened immunogenicity of T cell vaccines
    • Chen J-L, et al. Structural and kinetic basis for heightened immunogenicity of T cell vaccines. J Exp Med 2005;201:1243-1255.
    • (2005) J Exp Med , vol.201 , pp. 1243-1255
    • Chen, J.-L.1
  • 19
    • 10644239910 scopus 로고    scopus 로고
    • T Cell Cross-Reactivity and Conformational Changes during TCR Engagement
    • Lee JK, et al. T Cell Cross-Reactivity and Conformational Changes during TCR Engagement. J Exp Med 2004;200:1455-1466.
    • (2004) J Exp Med , vol.200 , pp. 1455-1466
    • Lee, J.K.1
  • 20
    • 77953742968 scopus 로고    scopus 로고
    • Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability
    • Burrows SR, et al. Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability. Proc Natl Acad Sci USA 2010;107:10608-10613.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10608-10613
    • Burrows, S.R.1
  • 21
    • 26444521752 scopus 로고    scopus 로고
    • Unraveling a hotspot for TCR Recognition on HLA-A2: evidence against the existence of peptide-independent TCR binding determinants
    • Gagnon SJ, et al. Unraveling a hotspot for TCR Recognition on HLA-A2: evidence against the existence of peptide-independent TCR binding determinants. J Mol Biol 2005;353:556-573.
    • (2005) J Mol Biol , vol.353 , pp. 556-573
    • Gagnon, S.J.1
  • 22
    • 0035809315 scopus 로고    scopus 로고
    • Identification of a crucial energetic footprint on the α1 helix of human histocompatibility leukocyte atigen (HLA)-A2 that provides functional interactions for recognition by Tax peptide/HLA-A2-specific T cell receptors
    • Baker BM, Turner RV, Gagnon SJ, Wiley DC, Biddison WE. Identification of a crucial energetic footprint on the α1 helix of human histocompatibility leukocyte atigen (HLA)-A2 that provides functional interactions for recognition by Tax peptide/HLA-A2-specific T cell receptors. J Exp Med 2001;193:551-562.
    • (2001) J Exp Med , vol.193 , pp. 551-562
    • Baker, B.M.1    Turner, R.V.2    Gagnon, S.J.3    Wiley, D.C.4    Biddison, W.E.5
  • 23
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: progress and challenges
    • DeLano WL. Unraveling hot spots in binding interfaces: progress and challenges. Curr Opin Struct Biol 2002;12:14-20.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 14-20
    • DeLano, W.L.1
  • 24
    • 27944449312 scopus 로고    scopus 로고
    • Extensive T cell receptor cross-reactivity on structurally diverse haptenated peptides presented by HLA-A2
    • Gagnon SJ, Turner RV, Shiue MG, Damirjian M, Biddison WE. Extensive T cell receptor cross-reactivity on structurally diverse haptenated peptides presented by HLA-A2. Mol Immunol 2006;43:346-356.
    • (2006) Mol Immunol , vol.43 , pp. 346-356
    • Gagnon, S.J.1    Turner, R.V.2    Shiue, M.G.3    Damirjian, M.4    Biddison, W.E.5
  • 25
    • 33748809527 scopus 로고    scopus 로고
    • T cell receptor recognition via cooperative conformational plasticity
    • Gagnon SJ, et al. T cell receptor recognition via cooperative conformational plasticity. J Mol Biol 2006;363:228-243.
    • (2006) J Mol Biol , vol.363 , pp. 228-243
    • Gagnon, S.J.1
  • 26
    • 82555168290 scopus 로고    scopus 로고
    • Disparate degrees of hypervariable loop flexibility control T-cell receptor cross-reactivity, specificity, and binding mechanism
    • Scott DR, Borbulevych OY, Piepenbrink KH, Corcelli SA, Baker BM. Disparate degrees of hypervariable loop flexibility control T-cell receptor cross-reactivity, specificity, and binding mechanism. J Mol Biol 2011;414:385-400.
    • (2011) J Mol Biol , vol.414 , pp. 385-400
    • Scott, D.R.1    Borbulevych, O.Y.2    Piepenbrink, K.H.3    Corcelli, S.A.4    Baker, B.M.5
  • 27
    • 79952743743 scopus 로고    scopus 로고
    • Conformational melding permits a conserved binding geometry in TCR recognition of foreign and self molecular mimics
    • Borbulevych OY, Piepenbrink KH, Baker BM. Conformational melding permits a conserved binding geometry in TCR recognition of foreign and self molecular mimics. J Immunol 2011;186:2950-2958.
    • (2011) J Immunol , vol.186 , pp. 2950-2958
    • Borbulevych, O.Y.1    Piepenbrink, K.H.2    Baker, B.M.3
  • 28
    • 70350094712 scopus 로고    scopus 로고
    • Fluorine substitutions in an antigenic peptide selectively modulate T-cell receptor binding in a minimally perturbing manner
    • Piepenbrink KH, et al. Fluorine substitutions in an antigenic peptide selectively modulate T-cell receptor binding in a minimally perturbing manner. Biochem J 2009;423:353-361.
    • (2009) Biochem J , vol.423 , pp. 353-361
    • Piepenbrink, K.H.1
  • 29
    • 71749112218 scopus 로고    scopus 로고
    • T cell receptor cross-reactivity directed by antigen-dependent tuning of peptide-MHC molecular flexibility
    • Borbulevych OY, et al. T cell receptor cross-reactivity directed by antigen-dependent tuning of peptide-MHC molecular flexibility. Immunity 2009;31:885-896.
    • (2009) Immunity , vol.31 , pp. 885-896
    • Borbulevych, O.Y.1
  • 30
    • 23744479535 scopus 로고    scopus 로고
    • How the T cell receptor sees antigen - a structural view
    • Garcia KC, Adams EJ. How the T cell receptor sees antigen - a structural view. Cell 2005;122:333-336.
    • (2005) Cell , vol.122 , pp. 333-336
    • Garcia, K.C.1    Adams, E.J.2
  • 31
    • 79960462110 scopus 로고    scopus 로고
    • A single T cell receptor bound to major histocompatibility complex class I and Class II glycoproteins reveals switchable TCR conformers
    • Yin L, et al. A single T cell receptor bound to major histocompatibility complex class I and Class II glycoproteins reveals switchable TCR conformers. Immunity 2011;35:23-33.
    • (2011) Immunity , vol.35 , pp. 23-33
    • Yin, L.1
  • 32
    • 37549038674 scopus 로고    scopus 로고
    • A new twist in TCR diversity revealed by a forbidden αβ TCR
    • McBeth C, et al. A new twist in TCR diversity revealed by a forbidden αβ TCR. J Mol Biol 2008;375:1306-1319.
    • (2008) J Mol Biol , vol.375 , pp. 1306-1319
    • McBeth, C.1
  • 33
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg EJ, Mariuzza RA. Molecular recognition in antibody-antigen complexes. Adv Protein Chem 2002;61:119-160.
    • (2002) Adv Protein Chem , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 34
    • 0031664697 scopus 로고    scopus 로고
    • Molecular mimicry and immune-mediated diseases
    • Oldstone MBA. Molecular mimicry and immune-mediated diseases. FASEB J 1998;12:1255-1265.
    • (1998) FASEB J , vol.12 , pp. 1255-1265
    • Oldstone, M.B.A.1
  • 35
    • 0037342405 scopus 로고    scopus 로고
    • Mimicking the way to autoimmunity: an evolving theory of sequence and structural homology
    • Kohm AP, Fuller KG, Miller SD. Mimicking the way to autoimmunity: an evolving theory of sequence and structural homology. Trends Microbiol 2003;11:101-105.
    • (2003) Trends Microbiol , vol.11 , pp. 101-105
    • Kohm, A.P.1    Fuller, K.G.2    Miller, S.D.3
  • 36
    • 0034988649 scopus 로고    scopus 로고
    • Structural basis of molecular mimicry
    • Wucherpfennig KW. Structural basis of molecular mimicry. J Autoimmun 2001;16:293-302.
    • (2001) J Autoimmun , vol.16 , pp. 293-302
    • Wucherpfennig, K.W.1
  • 37
    • 33746256846 scopus 로고    scopus 로고
    • Distinct orientation of the alloreactive monoclonal CD8 T cell activation program by three different peptide/MHC complexes
    • Auphan-Anezin N, et al. Distinct orientation of the alloreactive monoclonal CD8 T cell activation program by three different peptide/MHC complexes. Eur J Immunol 2006;36:1856-1866.
    • (2006) Eur J Immunol , vol.36 , pp. 1856-1866
    • Auphan-Anezin, N.1
  • 38
    • 26644468528 scopus 로고    scopus 로고
    • Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule
    • Li Y, Huang Y, Lue J, Quandt JA, Martin R, Mariuzza RA. Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule. EMBO J 2005;24:2968-2979.
    • (2005) EMBO J , vol.24 , pp. 2968-2979
    • Li, Y.1    Huang, Y.2    Lue, J.3    Quandt, J.A.4    Martin, R.5    Mariuzza, R.A.6
  • 39
    • 30044434744 scopus 로고    scopus 로고
    • Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state
    • Tobi D, Bahar I. Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state. Proc Natl Acad Sci USA 2005;102:18908-18913.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18908-18913
    • Tobi, D.1    Bahar, I.2
  • 40
    • 36549043024 scopus 로고    scopus 로고
    • Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
    • Bahar I, Chennubhotla C, Tobi D. Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation. Curr Opin Struct Biol 2007;17:633-640.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 633-640
    • Bahar, I.1    Chennubhotla, C.2    Tobi, D.3
  • 41
    • 34250001164 scopus 로고    scopus 로고
    • Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: a case study of antibodies
    • Keskin O. Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: a case study of antibodies. BMC Struct Biol 2007;7:1-11.
    • (2007) BMC Struct Biol , vol.7 , pp. 1-11
    • Keskin, O.1
  • 43
    • 84855767247 scopus 로고    scopus 로고
    • Dynamical characterization of two differentially disease associated MHC class I proteins in complex with viral and self-peptides
    • Narzi D, Becker CM, Fiorillo MT, Uchanska-Ziegler B, Ziegler A, Böckmann RA. Dynamical characterization of two differentially disease associated MHC class I proteins in complex with viral and self-peptides. J Mol Biol 2012;415:429-442.
    • (2012) J Mol Biol , vol.415 , pp. 429-442
    • Narzi, D.1    Becker, C.M.2    Fiorillo, M.T.3    Uchanska-Ziegler, B.4    Ziegler, A.5    Böckmann, R.A.6
  • 44
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of theα2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • Smith KJ, Reid SW, Stuart DI, McMichael AJ, Jones EY, Bell JI. An altered position of theα2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 1996;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
  • 45
    • 4344677515 scopus 로고    scopus 로고
    • The LILR family: modulators of innate and adaptive immune pathways in health and disease
    • Brown D, Trowsdale J, Allen R. The LILR family: modulators of innate and adaptive immune pathways in health and disease. Tissue Antigens 2004;64:215-225.
    • (2004) Tissue Antigens , vol.64 , pp. 215-225
    • Brown, D.1    Trowsdale, J.2    Allen, R.3
  • 47
    • 0036214286 scopus 로고    scopus 로고
    • Structure and function of antrual killer cell receptors: multiple molecular solutions to self, nonself discrimination
    • Natarajan K, Dimasi N, Wang J, Mariuzza RA, Margulies DH. Structure and function of antrual killer cell receptors: multiple molecular solutions to self, nonself discrimination. Annu Rev Immunol 2002;20:853-885.
    • (2002) Annu Rev Immunol , vol.20 , pp. 853-885
    • Natarajan, K.1    Dimasi, N.2    Wang, J.3    Mariuzza, R.A.4    Margulies, D.H.5
  • 48
    • 0347382594 scopus 로고    scopus 로고
    • Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2Kb
    • Dam J, et al. Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2Kb. Nat Immunol 2003;4:1213-1222.
    • (2003) Nat Immunol , vol.4 , pp. 1213-1222
    • Dam, J.1
  • 49
    • 80053061665 scopus 로고    scopus 로고
    • Recognition of class I MHC by a rat Ly49 NK cell receptor is dependent on the identity of the P2 anchor amino acid of bound peptide
    • Ma BJ, Kane KP. Recognition of class I MHC by a rat Ly49 NK cell receptor is dependent on the identity of the P2 anchor amino acid of bound peptide. J Immunol 2011;187:3267-3276.
    • (2011) J Immunol , vol.187 , pp. 3267-3276
    • Ma, B.J.1    Kane, K.P.2
  • 51
    • 81555213587 scopus 로고    scopus 로고
    • Killer cell immunoglobulin-like receptor 3DL1-mediated recognition of human leukocyte antigen B
    • Vivian JP, et al. Killer cell immunoglobulin-like receptor 3DL1-mediated recognition of human leukocyte antigen B. Nature 2011;479:401-405.
    • (2011) Nature , vol.479 , pp. 401-405
    • Vivian, J.P.1
  • 52
    • 0030926140 scopus 로고    scopus 로고
    • Crystal structure of the complex between human CD8alpha (alpha) and HLA- A2
    • Gao GF, et al. Crystal structure of the complex between human CD8alpha (alpha) and HLA- A2. Nature 1997;387:630-634.
    • (1997) Nature , vol.387 , pp. 630-634
    • Gao, G.F.1
  • 53
    • 70449470318 scopus 로고    scopus 로고
    • Structural alterations in peptide-MHC recognition by self-reactive T cell receptors
    • Wucherpfennig KW, Call MJ, Deng L, Mariuzza R. Structural alterations in peptide-MHC recognition by self-reactive T cell receptors. Curr Opin Immunol 2009;21:590-595.
    • (2009) Curr Opin Immunol , vol.21 , pp. 590-595
    • Wucherpfennig, K.W.1    Call, M.J.2    Deng, L.3    Mariuzza, R.4
  • 54
    • 26644447982 scopus 로고    scopus 로고
    • Unusual features of self-peptide/MHC binding by autoimmune T cell receptors
    • Nicholson MJ, Hahn M, Wucherpfennig KW. Unusual features of self-peptide/MHC binding by autoimmune T cell receptors. Immunity 2005;23:351-360.
    • (2005) Immunity , vol.23 , pp. 351-360
    • Nicholson, M.J.1    Hahn, M.2    Wucherpfennig, K.W.3
  • 55
    • 79952750632 scopus 로고    scopus 로고
    • Structure of a TCR with high affinity for self-antigen reveals basis for escape from negative selection
    • Yin Y, Li Y, Kerzic MC, Martin R, Mariuzza RA. Structure of a TCR with high affinity for self-antigen reveals basis for escape from negative selection. EMBO J 2011;30:1137-1148.
    • (2011) EMBO J , vol.30 , pp. 1137-1148
    • Yin, Y.1    Li, Y.2    Kerzic, M.C.3    Martin, R.4    Mariuzza, R.A.5
  • 56
    • 70350438026 scopus 로고    scopus 로고
    • Germline-governed recognition of a cancer epitope by an immunodominant human T-cell receptor
    • Cole DK, et al. Germline-governed recognition of a cancer epitope by an immunodominant human T-cell receptor. J Biol Chem 2009;284:27281-27289.
    • (2009) J Biol Chem , vol.284 , pp. 27281-27289
    • Cole, D.K.1
  • 57
    • 80052677601 scopus 로고    scopus 로고
    • TCRs used in cancer gene therapy cross-react with MART-1/Melan-A Tumor antigens via distinct mechanisms
    • Borbulevych OY, Santhanagopolan SM, Hossain M, Baker BM. TCRs used in cancer gene therapy cross-react with MART-1/Melan-A Tumor antigens via distinct mechanisms. J Immunol 2011;187:2453-2463.
    • (2011) J Immunol , vol.187 , pp. 2453-2463
    • Borbulevych, O.Y.1    Santhanagopolan, S.M.2    Hossain, M.3    Baker, B.M.4
  • 58
    • 0030935007 scopus 로고    scopus 로고
    • The MHC reactivity of the T cell repertoire prior to positive and negative selection
    • Zerrahn J, Held W, Raulet DH. The MHC reactivity of the T cell repertoire prior to positive and negative selection. Cell 1997;88:627-636.
    • (1997) Cell , vol.88 , pp. 627-636
    • Zerrahn, J.1    Held, W.2    Raulet, D.H.3
  • 59
    • 0036682133 scopus 로고    scopus 로고
    • Two-step binding mechanism for T-cell receptor recognition of peptide MHC
    • Wu LC, Tuot DS, Lyons DS, Garcia KC, Davis MM. Two-step binding mechanism for T-cell receptor recognition of peptide MHC. Nature 2002;418:552-556.
    • (2002) Nature , vol.418 , pp. 552-556
    • Wu, L.C.1    Tuot, D.S.2    Lyons, D.S.3    Garcia, K.C.4    Davis, M.M.5
  • 60
    • 1242270594 scopus 로고    scopus 로고
    • T cell receptors: affinities, cross-reactivities, and a conformer model
    • Holler PD, Kranz DM. T cell receptors: affinities, cross-reactivities, and a conformer model. Mol Immunol 2004;40:1027-1031.
    • (2004) Mol Immunol , vol.40 , pp. 1027-1031
    • Holler, P.D.1    Kranz, D.M.2
  • 61
    • 0033613074 scopus 로고    scopus 로고
    • Thermodynamics of T cell receptor binding to peptide-MHC: evidence for a general mechanism of molecular scanning
    • Boniface JJ, Reich Z, Lyons DS, Davis MM. Thermodynamics of T cell receptor binding to peptide-MHC: evidence for a general mechanism of molecular scanning. Proc Natl Acad Sci USA 1999;96:11446-11451.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11446-11451
    • Boniface, J.J.1    Reich, Z.2    Lyons, D.S.3    Davis, M.M.4
  • 62
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: an extended view of binding events
    • Csermely P, Palotai R, Nussinov R. Induced fit, conformational selection and independent dynamic segments: an extended view of binding events. Trends Biochem Sci 2010;35:539-546.
    • (2010) Trends Biochem Sci , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 63
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr DD, Nussinov R, Wright PE. The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 2009;5:789-796.
    • (2009) Nat Chem Biol , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 64
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James LC, Roversi P, Tawfik DS. Antibody multispecificity mediated by conformational diversity. Science 2003;299:1362-1367.
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 65
    • 24644521419 scopus 로고    scopus 로고
    • Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition
    • James LC, Tawfik DS. Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition. Proc Natl Acad Sci USA 2005;102:12730-12735.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12730-12735
    • James, L.C.1    Tawfik, D.S.2
  • 66
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • Foote J, Milstein C. Conformational isomerism and the diversity of antibodies. Proc Natl Acad Sci USA 1994;91:10370-10374.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 67
    • 2942659074 scopus 로고    scopus 로고
    • T cell receptor-ligand interactions: a conformational preequilibrium or an induced fit
    • Gakamsky DM, Luescher IF, Pecht I. T cell receptor-ligand interactions: a conformational preequilibrium or an induced fit. Proc Natl Acad Sci USA 2004;101:9063-9066.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9063-9066
    • Gakamsky, D.M.1    Luescher, I.F.2    Pecht, I.3
  • 68
    • 33947445379 scopus 로고
    • A theory of the structure and process of formation of antibodies
    • Pauling L. A theory of the structure and process of formation of antibodies. J Am Chem Soc 1940;62:2643-2657.
    • (1940) J Am Chem Soc , vol.62 , pp. 2643-2657
    • Pauling, L.1
  • 69
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-a 60-year-old hypothesis revisited
    • James LC, Tawfik DS. Conformational diversity and protein evolution-a 60-year-old hypothesis revisited. Trends Biochem Sci 2003;28:361-368.
    • (2003) Trends Biochem Sci , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 70
    • 54049111388 scopus 로고    scopus 로고
    • Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes
    • Armstrong KM, Piepenbrink KH, Baker BM. Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes. Biochem J 2008;415:183-196.
    • (2008) Biochem J , vol.415 , pp. 183-196
    • Armstrong, K.M.1    Piepenbrink, K.H.2    Baker, B.M.3
  • 71
    • 0033017466 scopus 로고    scopus 로고
    • Structure, specificity and CDR mobility of a class II restricted single-chain T-cell receptor
    • Hare BJ, Wyss DF, Osburne MS, Kern PS, Reinherz EL, Wagner G. Structure, specificity and CDR mobility of a class II restricted single-chain T-cell receptor. Nat Struct Biol 1999;6:574-581.
    • (1999) Nat Struct Biol , vol.6 , pp. 574-581
    • Hare, B.J.1    Wyss, D.F.2    Osburne, M.S.3    Kern, P.S.4    Reinherz, E.L.5    Wagner, G.6
  • 72
    • 33847021917 scopus 로고    scopus 로고
    • T cell receptor binding transition states and recognition of peptide/MHC
    • Davis-Harrison RL, Insaidoo FK, Baker BM. T cell receptor binding transition states and recognition of peptide/MHC. Biochemistry 2007;46:1840-1850.
    • (2007) Biochemistry , vol.46 , pp. 1840-1850
    • Davis-Harrison, R.L.1    Insaidoo, F.K.2    Baker, B.M.3
  • 73
    • 34447299949 scopus 로고    scopus 로고
    • A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction
    • Armstrong KM, Baker BM. A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction. Biophys J 2007;93:597-609.
    • (2007) Biophys J , vol.93 , pp. 597-609
    • Armstrong, K.M.1    Baker, B.M.2
  • 74
    • 12544253697 scopus 로고    scopus 로고
    • Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/MHC ligand
    • Davis-Harrison RL, Armstrong KM, Baker BM. Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/MHC ligand. J Mol Biol 2005;346:533-550.
    • (2005) J Mol Biol , vol.346 , pp. 533-550
    • Davis-Harrison, R.L.1    Armstrong, K.M.2    Baker, B.M.3
  • 75
    • 47649130715 scopus 로고    scopus 로고
    • Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities
    • Armstrong KM, Insaidoo FK, Baker BM. Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities. J Mol Recognit 2008;21:275-287.
    • (2008) J Mol Recognit , vol.21 , pp. 275-287
    • Armstrong, K.M.1    Insaidoo, F.K.2    Baker, B.M.3
  • 76
    • 36749009635 scopus 로고    scopus 로고
    • Kinetic evidence for a ligand-binding-induced conformational transition in the T cell receptor
    • Gakamsky DM, et al. Kinetic evidence for a ligand-binding-induced conformational transition in the T cell receptor. Proc Natl Acad Sci USA 2007;104:16639-16644.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16639-16644
    • Gakamsky, D.M.1
  • 78
    • 34248530182 scopus 로고    scopus 로고
    • Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor
    • Deng L, et al. Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor. Nat Immunol 2007;8:398-408.
    • (2007) Nat Immunol , vol.8 , pp. 398-408
    • Deng, L.1
  • 80
    • 34548128306 scopus 로고    scopus 로고
    • Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'
    • Feng D, Bond CJ, Ely LK, Maynard J, Garcia KC. Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'. Nat Immunol 2007;8:975-983.
    • (2007) Nat Immunol , vol.8 , pp. 975-983
    • Feng, D.1    Bond, C.J.2    Ely, L.K.3    Maynard, J.4    Garcia, K.C.5
  • 81
    • 0037240790 scopus 로고    scopus 로고
    • A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity
    • Kjer-Nielsen L, et al. A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity. Immunity 2003;18:53-64.
    • (2003) Immunity , vol.18 , pp. 53-64
    • Kjer-Nielsen, L.1
  • 82
    • 79955611721 scopus 로고    scopus 로고
    • Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy
    • Fabian H, Loll B, Huser H, Naumann D, Uchanska-Ziegler B, Ziegler A. Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy. FEBS J 2011;278:1713-1727.
    • (2011) FEBS J , vol.278 , pp. 1713-1727
    • Fabian, H.1    Loll, B.2    Huser, H.3    Naumann, D.4    Uchanska-Ziegler, B.5    Ziegler, A.6
  • 83
    • 38649106449 scopus 로고    scopus 로고
    • HLA-B27 subtypes differentially associated with disease exhibit conformational differences in solution
    • Fabian H, et al. HLA-B27 subtypes differentially associated with disease exhibit conformational differences in solution. J Mol Biol 2008;376:798-810.
    • (2008) J Mol Biol , vol.376 , pp. 798-810
    • Fabian, H.1
  • 84
    • 34247891741 scopus 로고    scopus 로고
    • More than one reason to rethink the use of peptides in vaccine design
    • Purcell AW, McCluskey J, Rossjohn J. More than one reason to rethink the use of peptides in vaccine design. Nat Rev Drug Discov 2007;6:404-414.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 404-414
    • Purcell, A.W.1    McCluskey, J.2    Rossjohn, J.3
  • 86
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden DR. The three-dimensional structure of peptide-MHC complexes. Annu Rev Immunol 1995;13:587-622.
    • (1995) Annu Rev Immunol , vol.13 , pp. 587-622
    • Madden, D.R.1
  • 87
    • 0030587077 scopus 로고    scopus 로고
    • Improved induction of melanoma-reactive CTL with peptides from the melanoma antigen gp100 modified at HLA-A*0201-binding residues
    • Parkhurst M, et al. Improved induction of melanoma-reactive CTL with peptides from the melanoma antigen gp100 modified at HLA-A*0201-binding residues. J Immunol 1996;157:2539-2548.
    • (1996) J Immunol , vol.157 , pp. 2539-2548
    • Parkhurst, M.1
  • 88
    • 4344582378 scopus 로고    scopus 로고
    • Poor immunogenicity of a self/tumor antigen derives from peptide/MHC-I instability and is independent of tolerance
    • Yu Z, et al. Poor immunogenicity of a self/tumor antigen derives from peptide/MHC-I instability and is independent of tolerance. J Clin Invest 2004;114:551-559.
    • (2004) J Clin Invest , vol.114 , pp. 551-559
    • Yu, Z.1
  • 89
    • 0031890206 scopus 로고    scopus 로고
    • Immunologic and therapeutic evaluation of a synthetic peptide vaccine for the treatment of patients with metastatic melanoma
    • Rosenberg SA, et al. Immunologic and therapeutic evaluation of a synthetic peptide vaccine for the treatment of patients with metastatic melanoma. Nat Med 1998;4:321-327.
    • (1998) Nat Med , vol.4 , pp. 321-327
    • Rosenberg, S.A.1
  • 90
    • 17044415359 scopus 로고    scopus 로고
    • Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design
    • Borbulevych OY, Baxter TK, Yu Z, Restifo NP, Baker BM. Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design. J Immunol 2005;174:4812-4820.
    • (2005) J Immunol , vol.174 , pp. 4812-4820
    • Borbulevych, O.Y.1    Baxter, T.K.2    Yu, Z.3    Restifo, N.P.4    Baker, B.M.5
  • 91
    • 0033609729 scopus 로고    scopus 로고
    • Mass-spectrometric evaluation of HLA-A*0201-associated peptides identifies dominant naturally processed forms of CTL epitopes from MART-1 and gp100
    • Skipper JCA, et al. Mass-spectrometric evaluation of HLA-A*0201-associated peptides identifies dominant naturally processed forms of CTL epitopes from MART-1 and gp100. Int J Cancer 1999;82:669-677.
    • (1999) Int J Cancer , vol.82 , pp. 669-677
    • Skipper, J.C.A.1
  • 92
    • 34548493428 scopus 로고    scopus 로고
    • Structures of MART-1 (26/27-35) peptide/HLA-A2 complexes reveal a remarkable disconnect between antigen structural homology and T cell recognition
    • Borbulevych OY, et al. Structures of MART-1 (26/27-35) peptide/HLA-A2 complexes reveal a remarkable disconnect between antigen structural homology and T cell recognition. J Mol Biol 2007;372:1123-1136.
    • (2007) J Mol Biol , vol.372 , pp. 1123-1136
    • Borbulevych, O.Y.1
  • 93
    • 38849196276 scopus 로고    scopus 로고
    • A novel population of human melanoma-specific CD8 T cells recognizes Melan-AMART-1 immunodominant nonapeptide but not the corresponding decapeptide
    • Derré L, et al. A novel population of human melanoma-specific CD8 T cells recognizes Melan-AMART-1 immunodominant nonapeptide but not the corresponding decapeptide. J Immunol 2007;179:7635-7645.
    • (2007) J Immunol , vol.179 , pp. 7635-7645
    • Derré, L.1
  • 94
    • 81155132239 scopus 로고    scopus 로고
    • Loss of T cell antigen recognition arising from changes in peptide and major histocompatibility complex protein flexibility
    • Insaidoo FK, Borbulevych OY, Hossain M, Santhanagopolan SM, Baxter TK, Baker BM. Loss of T cell antigen recognition arising from changes in peptide and major histocompatibility complex protein flexibility. J Biol Chem 2011;286:40163-40173.
    • (2011) J Biol Chem , vol.286 , pp. 40163-40173
    • Insaidoo, F.K.1    Borbulevych, O.Y.2    Hossain, M.3    Santhanagopolan, S.M.4    Baxter, T.K.5    Baker, B.M.6
  • 95
    • 0028302028 scopus 로고
    • Identification of the immunodominant peptides of the MART-1 human melanoma antigen recognized by the majority of HLA-A2-restricted tumor infiltrating lymphocytes
    • Kawakami Y, et al. Identification of the immunodominant peptides of the MART-1 human melanoma antigen recognized by the majority of HLA-A2-restricted tumor infiltrating lymphocytes. J Exp Med 1994;180:347-352.
    • (1994) J Exp Med , vol.180 , pp. 347-352
    • Kawakami, Y.1
  • 96
    • 0028942142 scopus 로고
    • Induction of tumor-reactive CTL from peripheral blood and tumor- infiltrating lymphocytes of melanoma patients by in vitro stimulation with an immunodominant peptide of the human melanoma antigen MART-1
    • Rivoltini L, et al. Induction of tumor-reactive CTL from peripheral blood and tumor- infiltrating lymphocytes of melanoma patients by in vitro stimulation with an immunodominant peptide of the human melanoma antigen MART-1. J Immunol 1995;154:2257-2265.
    • (1995) J Immunol , vol.154 , pp. 2257-2265
    • Rivoltini, L.1
  • 97
    • 77957926275 scopus 로고    scopus 로고
    • Crystal structures of HLA-A*0201 complexed with Melan-A/MART-1 (26 (27L)-35) peptidomimetics reveal conformational heterogeneity and highlight degeneracy of Tcell recognition
    • Douat-Casassus C, et al. Crystal structures of HLA-A*0201 complexed with Melan-A/MART-1 (26 (27L)-35) peptidomimetics reveal conformational heterogeneity and highlight degeneracy of Tcell recognition. J Med Chem 2010;53:7061-7066.
    • (2010) J Med Chem , vol.53 , pp. 7061-7066
    • Douat-Casassus, C.1
  • 98
    • 0035884987 scopus 로고    scopus 로고
    • Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes
    • Sliz P, et al. Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes. J Immunol 2001;167:3276-3284.
    • (2001) J Immunol , vol.167 , pp. 3276-3284
    • Sliz, P.1
  • 99
    • 77956914881 scopus 로고    scopus 로고
    • Modification of MHC anchor residues generates heteroclitic peptides that alter TCR binding and T cell recognition
    • Cole DK, et al. Modification of MHC anchor residues generates heteroclitic peptides that alter TCR binding and T cell recognition. J Immunol 2010;185:2600-2610.
    • (2010) J Immunol , vol.185 , pp. 2600-2610
    • Cole, D.K.1
  • 100
    • 41649119810 scopus 로고    scopus 로고
    • Unmodified self antigen triggers human CD8 T cells with stronger tumor reactivity than altered antigen
    • Speiser DE, et al. Unmodified self antigen triggers human CD8 T cells with stronger tumor reactivity than altered antigen. Proc Natl Acad Sci USA 2008;105:3849-3854.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3849-3854
    • Speiser, D.E.1
  • 101
    • 84858758766 scopus 로고    scopus 로고
    • Adoptive immunotherapy for cancer: harnessing the T cell response
    • Restifo NP, Dudley ME, Rosenberg SA. Adoptive immunotherapy for cancer: harnessing the T cell response. Nat Rev Immunol 2012;12:269-281.
    • (2012) Nat Rev Immunol , vol.12 , pp. 269-281
    • Restifo, N.P.1    Dudley, M.E.2    Rosenberg, S.A.3
  • 102
    • 84860611911 scopus 로고    scopus 로고
    • Genetic engineering with T cell receptors
    • Zhang L, Morgan RA. Genetic engineering with T cell receptors. Adv Drug Deliv Rev 2011;64:756-762.
    • (2011) Adv Drug Deliv Rev , vol.64 , pp. 756-762
    • Zhang, L.1    Morgan, R.A.2
  • 103
  • 104
    • 33749624177 scopus 로고    scopus 로고
    • Cancer regression in patients after transfer of genetically engineered lymphocytes
    • Morgan RA, et al. Cancer regression in patients after transfer of genetically engineered lymphocytes. Science 2006;314:126-129.
    • (2006) Science , vol.314 , pp. 126-129
    • Morgan, R.A.1
  • 105
    • 70149114880 scopus 로고    scopus 로고
    • Gene therapy with human and mouse T-cell receptors mediates cancer regression and targets normal tissues expressing cognate antigen
    • Johnson LA, et al. Gene therapy with human and mouse T-cell receptors mediates cancer regression and targets normal tissues expressing cognate antigen. Blood 2009;114:535-546.
    • (2009) Blood , vol.114 , pp. 535-546
    • Johnson, L.A.1
  • 106
    • 33750324618 scopus 로고    scopus 로고
    • Gene Transfer of tumor-reactive TCR confers both high avidity and tumor reactivity to nonreactive peripheral blood mononuclear cells and tumor-infiltrating lymphocytes
    • Johnson LA, et al. Gene Transfer of tumor-reactive TCR confers both high avidity and tumor reactivity to nonreactive peripheral blood mononuclear cells and tumor-infiltrating lymphocytes. J Immunol 2006;177:6548-6559.
    • (2006) J Immunol , vol.177 , pp. 6548-6559
    • Johnson, L.A.1
  • 107
    • 33947726614 scopus 로고    scopus 로고
    • How a single T cell receptor recognizes both self and foreign MHC
    • Colf LA, et al. How a single T cell receptor recognizes both self and foreign MHC. Cell 2007;129:135-146.
    • (2007) Cell , vol.129 , pp. 135-146
    • Colf, L.A.1
  • 110
    • 58649114309 scopus 로고    scopus 로고
    • The molecular basis of TCR germline bias for MHC is surprisingly simple
    • Garcia KC, Adams JJ, Feng D, Ely LK. The molecular basis of TCR germline bias for MHC is surprisingly simple. Nat Immunol 2009;10:143-147.
    • (2009) Nat Immunol , vol.10 , pp. 143-147
    • Garcia, K.C.1    Adams, J.J.2    Feng, D.3    Ely, L.K.4
  • 111
    • 0001937634 scopus 로고
    • The somatic generation of immune recognition
    • Jerne NK. The somatic generation of immune recognition. Eur J Immunol 1971;1:1-9.
    • (1971) Eur J Immunol , vol.1 , pp. 1-9
    • Jerne, N.K.1
  • 112
    • 67349280397 scopus 로고    scopus 로고
    • Germline-encoded amino acids in the [agr][bgr] T-cell receptor control thymic selection
    • Scott-Browne JP, White J, Kappler JW, Gapin L, Marrack P. Germline-encoded amino acids in the [agr][bgr] T-cell receptor control thymic selection. Nature 2009;458:1043-1046.
    • (2009) Nature , vol.458 , pp. 1043-1046
    • Scott-Browne, J.P.1    White, J.2    Kappler, J.W.3    Gapin, L.4    Marrack, P.5
  • 113
    • 62549102995 scopus 로고    scopus 로고
    • TCR-MHC docking orientation: natural selection, or thymic selection?
    • Collins E, Riddle D. TCR-MHC docking orientation: natural selection, or thymic selection? Immunol Res 2008;41:267-294.
    • (2008) Immunol Res , vol.41 , pp. 267-294
    • Collins, E.1    Riddle, D.2
  • 114
    • 36048942337 scopus 로고    scopus 로고
    • Deletion of CD4 and CD8 coreceptors permits generation of [alpha][beta]T cells that recognize antigens independently of the MHC
    • Van Laethem F, et al. Deletion of CD4 and CD8 coreceptors permits generation of [alpha][beta]T cells that recognize antigens independently of the MHC. Immunity 2007;27:735-750.
    • (2007) Immunity , vol.27 , pp. 735-750
    • Van Laethem, F.1
  • 115
    • 84856291875 scopus 로고    scopus 로고
    • αβ T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities
    • Tikhonova A, et al. αβ T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities. Immunity 2012;36:79-91.
    • (2012) Immunity , vol.36 , pp. 79-91
    • Tikhonova, A.1
  • 116
    • 81955164077 scopus 로고    scopus 로고
    • T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex
    • Adams Jarrett J, et al. T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex. Immunity 2011;35:681-693.
    • (2011) Immunity , vol.35 , pp. 681-693
    • Adams Jarrett, J.1
  • 117
    • 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 YH, Smith KJ, Garboczi DN, Utz U, Biddison WE, Wiley DC. Two human T cell receptors bind in a similar diagonal mode to the HLA- A2/Tax peptide complex using different TCR amino acids. Immunity 1998;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
  • 118
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins
    • Koide S, Sidhu SS. The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins. ACS Chem Biol 2009;4:325-334.
    • (2009) ACS Chem Biol , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 119
    • 40849097408 scopus 로고    scopus 로고
    • The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies
    • Birtalan S, Zhang Y, Fellouse FA, Shao L, Schaefer G, Sidhu SS. The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies. J Mol Biol 2008;377:1518-1528.
    • (2008) J Mol Biol , vol.377 , pp. 1518-1528
    • Birtalan, S.1    Zhang, Y.2    Fellouse, F.A.3    Shao, L.4    Schaefer, G.5    Sidhu, S.S.6
  • 120
    • 71749086109 scopus 로고    scopus 로고
    • The multiple mechanisms of T cell receptor cross-reactivity
    • Yin Y, Mariuzza RA. The multiple mechanisms of T cell receptor cross-reactivity. Immunity 2009;31:849-851.
    • (2009) Immunity , vol.31 , pp. 849-851
    • Yin, Y.1    Mariuzza, R.A.2
  • 121
    • 33644556820 scopus 로고    scopus 로고
    • Enzyme dynamics along the reaction coordinate: critical role of a conserved residue
    • Kovrigin EL, Loria JP. Enzyme dynamics along the reaction coordinate: critical role of a conserved residue. Biochemistry 2006;45:2636-2647.
    • (2006) Biochemistry , vol.45 , pp. 2636-2647
    • Kovrigin, E.L.1    Loria, J.P.2
  • 122
    • 3242755777 scopus 로고    scopus 로고
    • Tracing kinetic intermediates during ligand binding
    • Mittag T, Schaffhausen B, Günther UL. Tracing kinetic intermediates during ligand binding. J Am Chem Soc 2004;126:9017-9023.
    • (2004) J Am Chem Soc , vol.126 , pp. 9017-9023
    • Mittag, T.1    Schaffhausen, B.2    Günther, U.L.3
  • 123
    • 34548736431 scopus 로고    scopus 로고
    • Solution mapping of T cell receptor docking footprints on peptide-MHC
    • Varani L, et al. Solution mapping of T cell receptor docking footprints on peptide-MHC. Proc Natl Acad Sci USA 2007;104:13080-13085.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13080-13085
    • Varani, L.1
  • 124
    • 80053577815 scopus 로고    scopus 로고
    • Mass spectrometry: come of age for structural and dynamical biology
    • Benesch JLP, Ruotolo BT. Mass spectrometry: come of age for structural and dynamical biology. Curr Opin Struct Biol 2011;21:641-649.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 641-649
    • Benesch, J.L.P.1    Ruotolo, B.T.2
  • 125
    • 0037437910 scopus 로고    scopus 로고
    • A yeast display system for engineering functional peptide-MHC complexes
    • Brophy SE, Holler PD, Kranz DM. A yeast display system for engineering functional peptide-MHC complexes. J Immunol Methods 2003;272:235-246.
    • (2003) J Immunol Methods , vol.272 , pp. 235-246
    • Brophy, S.E.1    Holler, P.D.2    Kranz, D.M.3
  • 127
    • 57349118383 scopus 로고    scopus 로고
    • Control of HIV-1 immune escape by CD8 T cells expressing enhanced T-cell receptor
    • Varela-Rohena A, et al. Control of HIV-1 immune escape by CD8 T cells expressing enhanced T-cell receptor. Nat Med 2008;14:1390-1395.
    • (2008) Nat Med , vol.14 , pp. 1390-1395
    • Varela-Rohena, A.1
  • 128
    • 19944432399 scopus 로고    scopus 로고
    • Design of soluble recombinant T cell receptors for antigen targeting and T cell inhibition
    • Laugel B, et al. Design of soluble recombinant T cell receptors for antigen targeting and T cell inhibition. J Biol Chem 2005;280:1882-1892.
    • (2005) J Biol Chem , vol.280 , pp. 1882-1892
    • Laugel, B.1
  • 129
    • 84862589122 scopus 로고    scopus 로고
    • Cutting edge: evidence for a dynamically driven T cell signaling mechanism
    • Hawse WF, et al. Cutting edge: evidence for a dynamically driven T cell signaling mechanism. J Immunol 2012;188:5819-5823.
    • (2012) J Immunol , vol.188 , pp. 5819-5823
    • Hawse, W.F.1
  • 130
    • 84862636672 scopus 로고    scopus 로고
    • Interplay between T cell receptor binding kinetics and the level of cognate peptide presented by major histocompatibility complexes governs CD8+ T cell responsiveness
    • Irving M, et al. Interplay between T cell receptor binding kinetics and the level of cognate peptide presented by major histocompatibility complexes governs CD8+ T cell responsiveness. J Biol Chem 2012;287:23068-23078.
    • (2012) J Biol Chem , vol.287 , pp. 23068-23078
    • Irving, M.1
  • 131
    • 61449234107 scopus 로고    scopus 로고
    • Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC
    • Haidar JN, Pierce B, Yu Y, Tong W, Li M, Weng Z. Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC. Proteins: Struct, Funct, Bioinf 2009;74:948-960.
    • (2009) Proteins: Struct, Funct, Bioinf , vol.74 , pp. 948-960
    • Haidar, J.N.1    Pierce, B.2    Yu, Y.3    Tong, W.4    Li, M.5    Weng, Z.6
  • 133
    • 0037234768 scopus 로고    scopus 로고
    • TCRs with high affinity for foreign pMHC show self-reactivity
    • Holler PD, Chlewicki LK, Kranz DM. TCRs with high affinity for foreign pMHC show self-reactivity. Nat Immunol 2003;4:55-62.
    • (2003) Nat Immunol , vol.4 , pp. 55-62
    • Holler, P.D.1    Chlewicki, L.K.2    Kranz, D.M.3
  • 134
    • 38449104431 scopus 로고    scopus 로고
    • High-affinity TCRs generated by phage display provide CD4(+) T cells with the ability to recognize and kill tumor cell lines
    • Zhao Y, et al. High-affinity TCRs generated by phage display provide CD4(+) T cells with the ability to recognize and kill tumor cell lines. J Immunol 2007;179:5845-5854.
    • (2007) J Immunol , vol.179 , pp. 5845-5854
    • Zhao, Y.1


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