메뉴 건너뛰기




Volumn 163, Issue , 1998, Pages 187-196

Glimpses at the recognition of peptide/MHC complexes by T-cell antigen receptors

Author keywords

[No Author keywords available]

Indexed keywords

LYMPHOCYTE ANTIGEN RECEPTOR; T LYMPHOCYTE RECEPTOR;

EID: 0031817312     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1998.tb01197.x     Document Type: Review
Times cited : (22)

References (34)
  • 1
    • 0028956603 scopus 로고
    • Crystal structure of the β chain of a T cell antigen receptor
    • Bentley GA, Boulot G, Karjalainen K, Mariuzza RA. Crystal structure of the β chain of a T cell antigen receptor. Science 1995;267:1984-1987.
    • (1995) Science , vol.267 , pp. 1984-1987
    • Bentley, G.A.1    Boulot, G.2    Karjalainen, K.3    Mariuzza, R.A.4
  • 2
    • 0029417003 scopus 로고
    • Crystal structure of the Vα domain of a T cell antigen receptor
    • Fields BA, et al. Crystal structure of the Vα domain of a T cell antigen receptor. Science 1995;270:1821-1824.
    • (1995) Science , vol.270 , pp. 1821-1824
    • Fields, B.A.1
  • 3
    • 0030855425 scopus 로고    scopus 로고
    • The three-dimensional structure of a T-cell antigen receptor VαVβ heterodiraer reveals a novel arrangement of the Vβ domain
    • Housset D, Mazza G, Grégoire C, Piras C, Malissen B, Fontecilla-Camps JC. The three-dimensional structure of a T-cell antigen receptor VαVβ heterodiraer reveals a novel arrangement of the Vβ domain. EMBO J 1997;16:4205-4216.
    • (1997) EMBO J , vol.16 , pp. 4205-4216
    • Housset, D.1    Mazza, G.2    Grégoire, C.3    Piras, C.4    Malissen, B.5    Fontecilla-Camps, J.C.6
  • 4
    • 0031566433 scopus 로고    scopus 로고
    • Dual conformations of a T cell receptor Vα homodimer: Implications for variability in VαVβ domain association
    • Li H, Lebedeva MI, Ward ES, Mariuzza RA. Dual conformations of a T cell receptor Vα homodimer: implications for variability in VαVβ domain association. J Mol Biol 1997;269:385-394.
    • (1997) J Mol Biol , vol.269 , pp. 385-394
    • Li, H.1    Lebedeva, M.I.2    Ward, E.S.3    Mariuzza, R.A.4
  • 5
    • 0032472057 scopus 로고    scopus 로고
    • Atomic structure of an αβ T cell receptor (TCR) heterodimer in complex with an anti-TCR Fab fragment derived from a mitogenic antibody
    • Wang JH, et al. Atomic structure of an αβ T cell receptor (TCR) heterodimer in complex with an anti-TCR Fab fragment derived from a mitogenic antibody. EMBO J 1998;17:10-26.
    • (1998) EMBO J , vol.17 , pp. 10-26
    • Wang, J.H.1
  • 7
    • 0029662223 scopus 로고    scopus 로고
    • An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex
    • Garcia KC, et al. An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex. Science 1996;274:209-219.
    • (1996) Science , vol.274 , pp. 209-219
    • Garcia, K.C.1
  • 8
    • 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
  • 10
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily domains for surface recognition
    • Williams AF, Barclay AN. The immunoglobulin superfamily domains for surface recognition. Annu Rev Immunol 1988;6:381-405.
    • (1988) Annu Rev Immunol , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 11
    • 0022339938 scopus 로고
    • Domain association in immunoglobulin molecules. The packing of variable domains
    • Chothia C, Novotny J, Bruccoleri R, Karplus M. Domain association in immunoglobulin molecules. The packing of variable domains. J Mol Biol 1985;186:651-663.
    • (1985) J Mol Biol , vol.186 , pp. 651-663
    • Chothia, C.1    Novotny, J.2    Bruccoleri, R.3    Karplus, M.4
  • 12
    • 2642648459 scopus 로고
    • The outline structure of the T-cell αβ receptor
    • Chothia C, Boswell DR, Lesk AM. The outline structure of the T-cell αβ receptor. EMBO J 1988;7:3745-3755.
    • (1988) EMBO J , vol.7 , pp. 3745-3755
    • Chothia, C.1    Boswell, D.R.2    Lesk, A.M.3
  • 13
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is dose to that containing variable domains
    • Harpaz Y, Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is dose to that containing variable domains. J Mol Biol 1994;238:528-539.
    • (1994) J Mol Biol , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 14
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J Mol Biol 1994;242:309-320.
    • (1994) J Mol Biol , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 15
    • 0030926140 scopus 로고    scopus 로고
    • Crystal structure of the complex between CD8αα and HLA-A2
    • Gao GF, et al. Crystal structure of the complex between CD8αα and HLA-A2. Nature 1997;387:630-634.
    • (1997) Nature , vol.387 , pp. 630-634
    • Gao, G.F.1
  • 16
    • 0027973205 scopus 로고
    • More efficient positive selection of thymocytes in mice lacking terminal deoxynucleotidyl transferase
    • Gilfillan S, Waltzinger C, Benoist C, Mathis D. More efficient positive selection of thymocytes in mice lacking terminal deoxynucleotidyl transferase. Int Immunol 1994;6:1681-1686.
    • (1994) Int Immunol , vol.6 , pp. 1681-1686
    • Gilfillan, S.1    Waltzinger, C.2    Benoist, C.3    Mathis, D.4
  • 17
    • 0029552310 scopus 로고
    • Increased peptide promiscuity provides a rationale for the lack of N regions in the neonatal T cell repertoire
    • Gavin MA, Bevan MJ. Increased peptide promiscuity provides a rationale for the lack of N regions in the neonatal T cell repertoire. Immunity 1995;3:793-800.
    • (1995) Immunity , vol.3 , pp. 793-800
    • Gavin, M.A.1    Bevan, M.J.2
  • 18
    • 0031253811 scopus 로고    scopus 로고
    • Vα3.2 selection in MHC class I mutant mice. Evidence for an alternate orientation of TCR-MHC class I interaction
    • Sim BC, Travers PJ, Gascoigne NRJ. Vα3.2 selection in MHC class I mutant mice. Evidence for an alternate orientation of TCR-MHC class I interaction. J Immunol 1997;159:3322-3329.
    • (1997) J Immunol , vol.159 , pp. 3322-3329
    • Sim, B.C.1    Travers, P.J.2    Gascoigne, N.R.J.3
  • 19
    • 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
  • 21
    • 0031916706 scopus 로고    scopus 로고
    • Polymorphism within a TCRAV family influences the repertoire through class I/II restriction
    • Sim BC, Wung JL, Gascoigne NRJ. Polymorphism within a TCRAV family influences the repertoire through class I/II restriction. J Immunol 1998;160:1204-1211.
    • (1998) J Immunol , vol.160 , pp. 1204-1211
    • Sim, B.C.1    Wung, J.L.2    Gascoigne, N.R.J.3
  • 22
    • 0028926223 scopus 로고
    • Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein
    • Wucherpfennig KW, Strominger JL. Molecular mimicry in T cell-mediated autoimmunity: viral peptides activate human T cell clones specific for myelin basic protein. Cell 1995;80:695-705.
    • (1995) Cell , vol.80 , pp. 695-705
    • Wucherpfennig, K.W.1    Strominger, J.L.2
  • 23
    • 0028979705 scopus 로고
    • Specific T cell recognition of minimally homologous peptides: Evidence for multiple endogenous ligands
    • Evavold BD, Sloan-Lancaster J, Wilson KJ, Rothbard JB, Allen PM. Specific T cell recognition of minimally homologous peptides: evidence for multiple endogenous ligands. Immunity 1995;2:655-663.
    • (1995) Immunity , vol.2 , pp. 655-663
    • Evavold, B.D.1    Sloan-Lancaster, J.2    Wilson, K.J.3    Rothbard, J.B.4    Allen, P.M.5
  • 24
    • 0029961893 scopus 로고    scopus 로고
    • Structural basis for T cell recognition of altered peptide ligands: A single T cell receptor can productively recognize a large continuum of related ligands
    • Kersh GJ, Allen PM. Structural basis for T cell recognition of altered peptide ligands: a single T cell receptor can productively recognize a large continuum of related ligands. J Exp Med 1996;184:1259-1268.
    • (1996) J Exp Med , vol.184 , pp. 1259-1268
    • Kersh, G.J.1    Allen, P.M.2
  • 25
    • 0030950405 scopus 로고    scopus 로고
    • Identification of a naturally occurring ligand for thymic positive selection
    • Hogquist KA, et al. Identification of a naturally occurring ligand for thymic positive selection. Immunity 1997;6:389-399.
    • (1997) Immunity , vol.6 , pp. 389-399
    • Hogquist, K.A.1
  • 26
    • 0030865858 scopus 로고    scopus 로고
    • T cells can be activated by peptides that are unrelated in sequence to their selecting peptide
    • Ignatowicz L, et al. T cells can be activated by peptides that are unrelated in sequence to their selecting peptide. Immunity 1997;7:179-186.
    • (1997) Immunity , vol.7 , pp. 179-186
    • Ignatowicz, L.1
  • 27
    • 0031056062 scopus 로고    scopus 로고
    • Positive selection of T cells induced by viral delivery of neopeptides to the thymus
    • Nakano N, Rooke R, Benoist C, Mathis D. Positive selection of T cells induced by viral delivery of neopeptides to the thymus. Science 1997;275:678-683.
    • (1997) Science , vol.275 , pp. 678-683
    • Nakano, N.1    Rooke, R.2    Benoist, C.3    Mathis, D.4
  • 28
    • 0032078216 scopus 로고    scopus 로고
    • Quantitative aspects of T cell recognition: From within the antigen presenting cell to within the T cell
    • In press
    • Bongrand P, Malissen B. Quantitative aspects of T cell recognition: from within the antigen presenting cell to within the T cell. Bioessays 1998 (In press).
    • (1998) Bioessays
    • Bongrand, P.1    Malissen, B.2
  • 29
    • 0030873556 scopus 로고    scopus 로고
    • Differential requirements for survival and proliferation of CD8 naive or memory T cells
    • Tanchot C, Leinmonier FA, Pérarnau B, Freitas AA, Rocha B. Differential requirements for survival and proliferation of CD8 naive or memory T cells. Science 1997;276:2000-2001.
    • (1997) Science , vol.276 , pp. 2000-2001
    • Tanchot, C.1    Leinmonier, F.A.2    Pérarnau, B.3    Freitas, A.A.4    Rocha, B.5
  • 30
    • 0031454829 scopus 로고    scopus 로고
    • Crystallographic analysis of anti-p24 (HIV-1). Monoclonal antibody cross-reactivity and polyspecificity
    • Keitel T, Kramer A, Wessner H, Scholz C, Schneider-Mergener J, Hohne W. Crystallographic analysis of anti-p24 (HIV-1). Monoclonal antibody cross-reactivity and polyspecificity. Cell 1997;91:811-820.
    • (1997) Cell , vol.91 , pp. 811-820
    • Keitel, T.1    Kramer, A.2    Wessner, H.3    Scholz, C.4    Schneider-Mergener, J.5    Hohne, W.6
  • 32
    • 0030698234 scopus 로고    scopus 로고
    • The imprint of intrathymic self-peptides on the mature T cell receptor repertoire
    • Sant'Angelo DB, et al. The imprint of intrathymic self-peptides on the mature T cell receptor repertoire. Immunity 1997;7:517-524.
    • (1997) Immunity , vol.7 , pp. 517-524
    • Sant'Angelo, D.B.1
  • 34
    • 0030058657 scopus 로고    scopus 로고
    • The repertoire of T cells shaped by a single MHC/peptide ligand
    • Ignatowicz L, Kappler K, Marrack P. The repertoire of T cells shaped by a single MHC/peptide ligand. Cell 1996;84:521-529.
    • (1996) Cell , vol.84 , pp. 521-529
    • Ignatowicz, L.1    Kappler, K.2    Marrack, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.