메뉴 건너뛰기




Volumn 109, Issue 14, 2012, Pages 5405-5410

Crystal structure of a complete ternary complex of T-cell receptor, peptide-MHC, and CD4

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; HLA DR4 ANTIGEN; T LYMPHOCYTE RECEPTOR; TERNARY COMPLEX FACTOR;

EID: 84859470532     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1118801109     Document Type: Article
Times cited : (103)

References (48)
  • 1
    • 0026681679 scopus 로고
    • The T cell receptor as a multicomponent signalling machine: CD4/CD8 coreceptors and CD45 in T cell activation
    • Janeway CA, Jr. (1992) The T cell receptor as a multicomponent signalling machine: CD4/CD8 coreceptors and CD45 in T cell activation. Annu Rev Immunol 10:645-674.
    • (1992) Annu Rev Immunol , vol.10 , pp. 645-674
    • Janeway Jr., C.A.1
  • 2
    • 0037167816 scopus 로고    scopus 로고
    • Direct observation of ligand recognition by T cells
    • DOI 10.1038/nature01076
    • Irvine DJ, Purbhoo MA, Krogsgaard M, Davis MM (2002) Direct observation of ligand recognition by T cells. Nature 419:845-849. (Pubitemid 35238571)
    • (2002) Nature , vol.419 , Issue.6909 , pp. 845-849
    • Irvine, D.J.1    Purbhoo, M.A.2    Krogsgaard, M.3    Davis, M.M.4
  • 3
    • 0037331525 scopus 로고    scopus 로고
    • Quantitative analysis of the contribution of TCR/pepMHC affinity and CD8 to T cell activation
    • DOI 10.1016/S1074-7613(03)00019-0
    • Holler PD, Kranz DM (2003) Quantitative analysis of the contribution of TCR/pepMHC affinity and CD8 to T cell activation. Immunity 18:255-264. (Pubitemid 36263000)
    • (2003) Immunity , vol.18 , Issue.2 , pp. 255-264
    • Holler, P.D.1    Kranz, D.M.2
  • 4
    • 0027257445 scopus 로고
    • A kinase-independent function of Lck in potentiating antigen-specific T cell activation
    • DOI 10.1016/0092-8674(93)90511-N
    • Xu H, Littman DR (1993) A kinase-independent function of Lck in potentiating antigen-specific T cell activation. Cell 74:633-643. (Pubitemid 23259744)
    • (1993) Cell , vol.74 , Issue.4 , pp. 633-643
    • Xu, H.1    Littman, D.R.2
  • 5
    • 4444298148 scopus 로고    scopus 로고
    • CD4 enhances T cell sensitivity to antigen by coordinating Lck accumulation at the immunological synapse
    • Li QJ, et al. (2004) CD4 enhances T cell sensitivity to antigen by coordinating Lck accumulation at the immunological synapse. Nat Immunol 5:791-799.
    • (2004) Nat Immunol , vol.5 , pp. 791-799
    • Li, Q.J.1
  • 7
    • 78751696945 scopus 로고    scopus 로고
    • Two-stage cooperative T cell receptor-peptide major histocompatibility complex-CD8 trimolecular interactions amplify antigen discrimination
    • Jiang N, et al. (2011) Two-stage cooperative T cell receptor-peptide major histocompatibility complex-CD8 trimolecular interactions amplify antigen discrimination. Immunity 34:13-23.
    • (2011) Immunity , vol.34 , pp. 13-23
    • Jiang, N.1
  • 8
    • 78751683710 scopus 로고    scopus 로고
    • Late arrival: Recruiting coreceptors to the T cell receptor complex
    • van der Merwe PA, Cordoba SP (2011) Late arrival: Recruiting coreceptors to the T cell receptor complex. Immunity 34:1-3.
    • (2011) Immunity , vol.34 , pp. 1-3
    • Van Der Merwe, P.A.1    Cordoba, S.P.2
  • 10
    • 42649112362 scopus 로고    scopus 로고
    • Evolutionarily conserved amino acids that control TCR-MHC interaction
    • DOI 10.1146/annurev.immunol.26.021607.090421
    • Marrack P, Scott-Browne JP, Dai S, Gapin L, Kappler JW (2008) Evolutionarily conserved amino acids that control TCR-MHC interaction. Annu Rev Immunol 26:171-203. (Pubitemid 351600374)
    • (2008) Annual Review of Immunology , vol.26 , pp. 171-203
    • Marrack, P.1    Scott-Browne, J.P.2    Dai, S.3    Gapin, L.4    Kappler, J.W.5
  • 11
    • 70449470318 scopus 로고    scopus 로고
    • Structural alterations in peptide-MHC recognition by self-reactive T cell receptors
    • Wucherpfennig KW, Call MJ, Deng L, Mariuzza RA (2009) Structural alterations in peptide-MHC recognition by self-reactive T cell receptors. Curr Opin Immunol 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.A.4
  • 12
    • 0035845583 scopus 로고    scopus 로고
    • Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule
    • Wang JH, et al. (2001) Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule. Proc Natl Acad Sci USA 98:10799-10804.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10799-10804
    • Wang, J.H.1
  • 14
    • 15044358353 scopus 로고    scopus 로고
    • Agonist/endogenous peptide-MHC heterodimers drive T cell activation and sensitivity
    • DOI 10.1038/nature03391
    • Krogsgaard M, et al. (2005) Agonist/endogenous peptide-MHC heterodimers drive T cell activation and sensitivity. Nature 434:238-243. (Pubitemid 40388057)
    • (2005) Nature , vol.434 , Issue.7030 , pp. 238-243
    • Krogsgaard, M.1    Li, Q.-J.2    Sumen, C.3    Huppa, J.B.4    Huse, M.5    Davis, M.M.6
  • 15
    • 0030911709 scopus 로고    scopus 로고
    • Dimeric association and segmental variability in the structure of human CD4
    • DOI 10.1038/387527a0
    • Wu H, Kwong PD, Hendrickson WA (1997) Dimeric association and segmental variability in the structure of human CD4. Nature 387:527-530. (Pubitemid 27235474)
    • (1997) Nature , vol.387 , Issue.6632 , pp. 527-530
    • Wu, H.1    Kwong, P.D.2    Hendrickson, W.A.3
  • 16
    • 41449119309 scopus 로고    scopus 로고
    • Conformational rearrangement within the soluble domains of the CD4 receptor is ligand-specific
    • Ashish, et al. (2008) Conformational rearrangement within the soluble domains of the CD4 receptor is ligand-specific. J Biol Chem 283:2761-2772.
    • (2008) J Biol Chem , vol.283 , pp. 2761-2772
    • Ashish1
  • 17
    • 78650599246 scopus 로고    scopus 로고
    • Mechanisms for T cell receptor triggering
    • van der Merwe PA, Dushek O (2011) Mechanisms for T cell receptor triggering. Nat Rev Immunol 11:47-55.
    • (2011) Nat Rev Immunol , vol.11 , pp. 47-55
    • Van Der Merwe, P.A.1    Dushek, O.2
  • 19
    • 77950426522 scopus 로고    scopus 로고
    • Evidence for a functional sidedness to the alphabetaTCR
    • Kuhns MS, et al. (2010) Evidence for a functional sidedness to the alphabetaTCR. Proc Natl Acad Sci USA 107:5094-5099.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5094-5099
    • Kuhns, M.S.1
  • 20
    • 34548128306 scopus 로고    scopus 로고
    • Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'
    • DOI 10.1038/ni1502, PII NI1502
    • Feng D, Bond CJ, Ely LK, Maynard J, Garcia KC (2007) Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'. Nat Immunol 8:975-983. (Pubitemid 47300012)
    • (2007) Nature Immunology , vol.8 , Issue.9 , pp. 975-983
    • Feng, D.1    Bond, C.J.2    Ely, L.K.3    Maynard, J.4    Garcia, K.C.5
  • 21
    • 67349280397 scopus 로고    scopus 로고
    • Germline-encoded amino acids in the alphabeta T-cell receptor control thymic selection
    • Scott-Browne JP, White J, Kappler JW, Gapin L, Marrack P (2009) Germline-encoded amino acids in the alphabeta T-cell receptor control thymic selection. Nature 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
  • 22
    • 81955164077 scopus 로고    scopus 로고
    • T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex
    • Adams JJ, et al. (2011) T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex. Immunity 35:681-693.
    • (2011) Immunity , vol.35 , pp. 681-693
    • Adams, J.J.1
  • 23
    • 34447292366 scopus 로고    scopus 로고
    • What guides MHC-restricted TCR recognition?
    • DOI 10.1016/j.smim.2007.03.003, PII S1044532307000310, The Structure and Function of Antigen Receptors
    • Mazza C, Malissen B (2007) What guides MHC-restricted TCR recognition? Semin Immunol 19:225-235. (Pubitemid 47044975)
    • (2007) Seminars in Immunology , vol.19 , Issue.4 , pp. 225-235
    • Mazza, C.1    Malissen, B.2
  • 24
    • 0142219443 scopus 로고    scopus 로고
    • A correlation between TCR Valpha docking on MHC and CD8 dependence: Implications for T cell selection
    • DOI 10.1016/S1074-7613(03)00269-3
    • Buslepp J, Wang H, Biddison WE, Appella E, Collins EJ (2003) A correlation between TCR Valpha docking on MHC and CD8 dependence: Implications for T cell selection. Immunity 19:595-606. (Pubitemid 37311440)
    • (2003) Immunity , vol.19 , Issue.4 , pp. 595-606
    • Buslepp, J.1    Wang, H.2    Biddison, W.E.3    Appella, E.4    Collins, E.J.5
  • 26
    • 0035937132 scopus 로고    scopus 로고
    • T cell receptor binding to a pMHCII ligand is kinetically distinct from and independent of CD4
    • Xiong Y, Kern P, Chang H, Reinherz E (2001) T cell receptor binding to a pMHCII ligand is kinetically distinct from and independent of CD4. J Biol Chem 276:5659-5667.
    • (2001) J Biol Chem , vol.276 , pp. 5659-5667
    • Xiong, Y.1    Kern, P.2    Chang, H.3    Reinherz, E.4
  • 27
    • 80053152162 scopus 로고    scopus 로고
    • Affinity maturation of human CD4 by yeast surface display and crystal structure of a CD4-HLA-DR1 complex
    • Wang XX, et al. (2011) Affinity maturation of human CD4 by yeast surface display and crystal structure of a CD4-HLA-DR1 complex. Proc Natl Acad Sci USA 108:15960-15965.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 15960-15965
    • Wang, X.X.1
  • 28
    • 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 (2011) Structure of a TCR with high affinity for self-antigen reveals basis for escape from negative selection. EMBO J 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
  • 29
    • 33646859763 scopus 로고    scopus 로고
    • Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC
    • Maekawa A, Schmidt B, Fazekas de St Groth B, Sanejouand YH, Hogg PJ (2006) Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC. J Immunol 176:6873-6878. (Pubitemid 43787868)
    • (2006) Journal of Immunology , vol.176 , Issue.11 , pp. 6873-6878
    • Maekawa, A.1    Schmidt, B.2    De St., G.B.F.3    Sanejouand, Y.-H.4    Hogg, P.J.5
  • 30
    • 77249114784 scopus 로고    scopus 로고
    • TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity
    • Huppa JB, et al. (2010) TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity. Nature 463:963-967.
    • (2010) Nature , vol.463 , pp. 963-967
    • Huppa, J.B.1
  • 31
    • 33947173844 scopus 로고    scopus 로고
    • Disruption of Extracellular Interactions Impairs T Cell Receptor-CD3 Complex Stability and Signaling
    • DOI 10.1016/j.immuni.2007.01.015, PII S107476130700177X
    • Kuhns MS, Davis MM (2007) Disruption of extracellular interactions impairs T cell receptor-CD3 complex stability and signaling. Immunity 26:357-369. (Pubitemid 46413907)
    • (2007) Immunity , vol.26 , Issue.3 , pp. 357-369
    • Kuhns, M.S.1    Davis, M.M.2
  • 32
    • 84859447015 scopus 로고    scopus 로고
    • The T-cell receptor is a structure capable of initiating signalling in the absence of large conformational rearrangements
    • 2012 Jan 19 in press
    • Fernandes RA, et al. (2012) The T-cell receptor is a structure capable of initiating signalling in the absence of large conformational rearrangements. J Biol Chem 2012 Jan 19 (in press).
    • (2012) J Biol Chem
    • Fernandes, R.A.1
  • 33
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3å cytoplasmic tyrosine-based motif
    • Xu C, et al. (2008) Regulation of T cell receptor activation by dynamic membrane binding of the CD3å cytoplasmic tyrosine-based motif. Cell 135:702-713.
    • (2008) Cell , vol.135 , pp. 702-713
    • Xu, C.1
  • 34
    • 0030916713 scopus 로고    scopus 로고
    • Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface
    • DOI 10.1038/387312a0
    • Casasnovas JM, Springer TA, Liu JH, Harrison SC, Wang JH (1997) Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface. Nature 387:312-315. (Pubitemid 27220770)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 312-315
    • Casasnovas, J.M.1    Springer, T.A.2    Liu, J.-H.3    Harrison, S.C.4    Wang, J.-H.5
  • 35
    • 0036885014 scopus 로고    scopus 로고
    • CD4 dimers constitute the functional component required for T cell activation
    • Moldovan MC, et al. (2002) CD4 dimers constitute the functional component required for T cell activation. J Immunol 169:6261-6268.
    • (2002) J Immunol , vol.169 , pp. 6261-6268
    • Moldovan, M.C.1
  • 36
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • Ghosh P, Amaya M, Mellins E, Wiley DC (1995) The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378:457-462.
    • (1995) Nature , vol.378 , pp. 457-462
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 38
    • 18244392426 scopus 로고    scopus 로고
    • Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor
    • DOI 10.1038/ni1187
    • Hahn M, Nicholson MJ, Pyrdol J, Wucherpfennig KW (2005) Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor. Nat Immunol 6:490-496. (Pubitemid 41716762)
    • (2005) Nature Immunology , vol.6 , Issue.5 , pp. 490-496
    • Hahn, M.1    Nicholson, M.J.2    Pyrdol, J.3    Wucherpfennig, K.W.4
  • 39
    • 33644837787 scopus 로고    scopus 로고
    • Glycosylation and the function of the T cell co-receptor CD8
    • Shore DA, Wilson IA, Dwek RA, Rudd PM (2005) Glycosylation and the function of the T cell co-receptor CD8. Adv Exp Med Biol 564:71-84.
    • (2005) Adv Exp Med Biol , vol.564 , pp. 71-84
    • Shore, D.A.1    Wilson, I.A.2    Dwek, R.A.3    Rudd, P.M.4
  • 40
    • 0024389522 scopus 로고
    • Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: Light-scattering studies of ovine submaxillary mucin
    • Shogren R, Gerken TA, Jentoft N (1989) Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: Light-scattering studies of ovine submaxillary mucin. Biochemistry 28:5525-5536. (Pubitemid 19175764)
    • (1989) Biochemistry , vol.28 , Issue.13 , pp. 5525-5536
    • Shogren, R.1    Gerken, T.A.2    Jentoft, N.3
  • 41
    • 0024319438 scopus 로고
    • Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: Carbon-13 NMR studies of ovine submaxillary mucin
    • Gerken TA, Butenhof KJ, Shogren R (1989) Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: Carbon-13 NMR studies of ovine submaxillary mucin. Biochemistry 28:5536-5543. (Pubitemid 19175765)
    • (1989) Biochemistry , vol.28 , Issue.13 , pp. 5536-5543
    • Gerken, T.A.1    Butenhof, K.J.2    Shogren, R.3
  • 43
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • DOI 10.1038/sj.onc.1208081
    • Boggon TJ, Eck MJ (2004) Structure and regulation of Src family kinases. Oncogene 23:7918-7927. (Pubitemid 39468851)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 45
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54:905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 46
    • 77951623055 scopus 로고    scopus 로고
    • Super-resolution biomolecular crystallography with low-resolution data
    • Schröder GF, Levitt M, Brünger AT (2010) Super-resolution biomolecular crystallography with low-resolution data. Nature 464:1218-1222.
    • (2010) Nature , vol.464 , pp. 1218-1222
    • Schröder, G.F.1    Levitt, M.2    Brünger, A.T.3
  • 48
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66:213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.