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Volumn 8, Issue 3, 2012, Pages

Epitope flexibility and dynamic footprint revealed by molecular dynamics of a pMHC-TCR complex

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; MOLECULAR DYNAMICS; MOLECULES; T-CELLS;

EID: 84861128851     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002404     Document Type: Article
Times cited : (51)

References (47)
  • 1
    • 0036550559 scopus 로고    scopus 로고
    • Effector and memory T-cell differentiation: implications for vaccine development
    • Kaech SM, Wherry EJ, Ahmed R, (2002) Effector and memory T-cell differentiation: implications for vaccine development. Nat Rev Immunol 2: 251-262.
    • (2002) Nat Rev Immunol , vol.2 , pp. 251-262
    • Kaech, S.M.1    Wherry, E.J.2    Ahmed, R.3
  • 3
    • 0037237830 scopus 로고    scopus 로고
    • Not just any T cell receptor will do
    • Bankovich AJ, Garcia KC, (2003) Not just any T cell receptor will do. Immunity 18: 7-11.
    • (2003) Immunity , vol.18 , pp. 7-11
    • Bankovich, A.J.1    Garcia, K.C.2
  • 4
    • 66049132446 scopus 로고    scopus 로고
    • Many different Vbeta CDR3s can reveal the inherent MHC reactivity of germline-encoded TCR V regions
    • Rubtsova K, Scott-Browne JP, Crawford F, Dai S, Marrack P, et al. (2009) Many different Vbeta CDR3s can reveal the inherent MHC reactivity of germline-encoded TCR V regions. Proc Natl Acad Sci U S A 106: 7951-7956.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7951-7956
    • Rubtsova, K.1    Scott-Browne, J.P.2    Crawford, F.3    Dai, S.4    Marrack, P.5
  • 6
    • 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, (2007) Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'. Nat Immunol 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
  • 7
    • 56749129719 scopus 로고    scopus 로고
    • Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation
    • Jones LL, Colf LA, Stone JD, Garcia KC, Kranz DM, (2008) Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation. J Immunol 181: 6255-6264.
    • (2008) J Immunol , vol.181 , pp. 6255-6264
    • Jones, L.L.1    Colf, L.A.2    Stone, J.D.3    Garcia, K.C.4    Kranz, D.M.5
  • 8
    • 40249118205 scopus 로고    scopus 로고
    • Crossreactive T Cells spotlight the germline rules for alphabeta T cell-receptor interactions with MHC molecules
    • Dai S, Huseby ES, Rubtsova K, Scott-Browne J, Crawford F, et al. (2008) Crossreactive T Cells spotlight the germline rules for alphabeta T cell-receptor interactions with MHC molecules. Immunity 28: 324-334.
    • (2008) Immunity , vol.28 , pp. 324-334
    • Dai, S.1    Huseby, E.S.2    Rubtsova, K.3    Scott-Browne, J.4    Crawford, F.5
  • 9
    • 54049111388 scopus 로고    scopus 로고
    • Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes
    • Armstrong KM, Piepenbrink KH, Baker BM, (2008) Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes. Biochem J 415: 183-196.
    • (2008) Biochem J , vol.415 , pp. 183-196
    • Armstrong, K.M.1    Piepenbrink, K.H.2    Baker, B.M.3
  • 10
    • 78651076742 scopus 로고    scopus 로고
    • Evolving concepts of specificity in immune reactions
    • Eisen HN, Chakraborty AK, (2010) Evolving concepts of specificity in immune reactions. Proc Natl Acad Sci U S A 107: 22373-22380.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22373-22380
    • Eisen, H.N.1    Chakraborty, A.K.2
  • 11
    • 2942659074 scopus 로고    scopus 로고
    • T cell receptor-ligand interactions: a conformational preequilibrium or an induced fit
    • Gakamsky DM, Luescher IF, Pecht I, (2004) T cell receptor-ligand interactions: a conformational preequilibrium or an induced fit. Proc Natl Acad Sci U S A 101: 9063-9066.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9063-9066
    • Gakamsky, D.M.1    Luescher, I.F.2    Pecht, I.3
  • 12
    • 0034903068 scopus 로고    scopus 로고
    • The impact of duration versus extent of TCR occupancy on T cell activation: a revision of the kinetic proofreading model
    • Rosette C, Werlen G, Daniels MA, Holman PO, Alam SM, et al. (2001) The impact of duration versus extent of TCR occupancy on T cell activation: a revision of the kinetic proofreading model. Immunity 15: 59-70.
    • (2001) Immunity , vol.15 , pp. 59-70
    • Rosette, C.1    Werlen, G.2    Daniels, M.A.3    Holman, P.O.4    Alam, S.M.5
  • 13
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • McKeithan TW, (1995) Kinetic proofreading in T-cell receptor signal transduction. Proc Natl Acad Sci U S A 92: 5042-5046.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5042-5046
    • McKeithan, T.W.1
  • 14
    • 38449086723 scopus 로고    scopus 로고
    • CD8+ T cell activation is governed by TCR-peptide/MHC affinity, not dissociation rate
    • Tian S, Maile R, Collins EJ, Frelinger JA, (2007) CD8+ T cell activation is governed by TCR-peptide/MHC affinity, not dissociation rate. J Immunol 179: 2952-2960.
    • (2007) J Immunol , vol.179 , pp. 2952-2960
    • Tian, S.1    Maile, R.2    Collins, E.J.3    Frelinger, J.A.4
  • 16
    • 34247519546 scopus 로고    scopus 로고
    • The half-life of the T-cell receptor/peptide-major histocompatibility complex interaction can modulate T-cell activation in response to bacterial challenge
    • Carreno LJ, Bueno SM, Bull P, Nathenson SG, Kalergis AM, (2007) The half-life of the T-cell receptor/peptide-major histocompatibility complex interaction can modulate T-cell activation in response to bacterial challenge. Immunology 121: 227-237.
    • (2007) Immunology , vol.121 , pp. 227-237
    • Carreno, L.J.1    Bueno, S.M.2    Bull, P.3    Nathenson, S.G.4    Kalergis, A.M.5
  • 17
    • 4644272170 scopus 로고    scopus 로고
    • Potent T cell response to a class I-binding 13-mer viral epitope and the influence of HLA micropolymorphism in controlling epitope length
    • Green KJ, Miles JJ, Tellam J, van Zuylen WJ, Connolly G, et al. (2004) Potent T cell response to a class I-binding 13-mer viral epitope and the influence of HLA micropolymorphism in controlling epitope length. Eur J Immunol 34: 2510-2519.
    • (2004) Eur J Immunol , vol.34 , pp. 2510-2519
    • Green, K.J.1    Miles, J.J.2    Tellam, J.3    van Zuylen, W.J.4    Connolly, G.5
  • 18
    • 21244484755 scopus 로고    scopus 로고
    • High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance
    • Tynan FE, Borg NA, Miles JJ, Beddoe T, El-Hassen D, et al. (2005) High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance. J Biol Chem 280: 23900-23909.
    • (2005) J Biol Chem , vol.280 , pp. 23900-23909
    • Tynan, F.E.1    Borg, N.A.2    Miles, J.J.3    Beddoe, T.4    El-Hassen, D.5
  • 19
    • 27544446623 scopus 로고    scopus 로고
    • T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide
    • Tynan FE, Burrows SR, Buckle AM, Clements CS, Borg NA, et al. (2005) T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide. Nat Immunol 6: 1114-1122.
    • (2005) Nat Immunol , vol.6 , pp. 1114-1122
    • Tynan, F.E.1    Burrows, S.R.2    Buckle, A.M.3    Clements, C.S.4    Borg, N.A.5
  • 20
    • 0026728457 scopus 로고
    • Emerging principles for the recognition of peptide antigens by MHC class I molecules
    • Matsumura M, Fremont DH, Peterson PA, Wilson IA, (1992) Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257: 927-934.
    • (1992) Science , vol.257 , pp. 927-934
    • Matsumura, M.1    Fremont, D.H.2    Peterson, P.A.3    Wilson, I.A.4
  • 21
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the alpha 2 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, et al. (1996) An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 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
  • 22
    • 0033556246 scopus 로고    scopus 로고
    • Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus
    • Menssen R, Orth P, Ziegler A, Saenger W, (1999) Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus. J Mol Biol 285: 645-653.
    • (1999) J Mol Biol , vol.285 , pp. 645-653
    • Menssen, R.1    Orth, P.2    Ziegler, A.3    Saenger, W.4
  • 23
    • 3142543331 scopus 로고    scopus 로고
    • Differential peptide dynamics is linked to major histocompatibility complex polymorphism
    • Pohlmann T, Bockmann RA, Grubmuller H, Uchanska-Ziegler B, Ziegler A, et al. (2004) Differential peptide dynamics is linked to major histocompatibility complex polymorphism. J Biol Chem 279: 28197-28201.
    • (2004) J Biol Chem , vol.279 , pp. 28197-28201
    • Pohlmann, T.1    Bockmann, R.A.2    Grubmuller, H.3    Uchanska-Ziegler, B.4    Ziegler, A.5
  • 24
    • 71749112218 scopus 로고    scopus 로고
    • T cell receptor cross-reactivity directed by antigen-dependent tuning of peptide-MHC molecular flexibility
    • Borbulevych OY, Piepenbrink KH, Gloor BE, Scott DR, Sommese RF, et al. (2009) T cell receptor cross-reactivity directed by antigen-dependent tuning of peptide-MHC molecular flexibility. Immunity 31: 885-896.
    • (2009) Immunity , vol.31 , pp. 885-896
    • Borbulevych, O.Y.1    Piepenbrink, K.H.2    Gloor, B.E.3    Scott, D.R.4    Sommese, R.F.5
  • 25
    • 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, et al. (2011) Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy. FEBS J 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
  • 26
    • 38649106449 scopus 로고    scopus 로고
    • HLA-B27 subtypes differentially associated with disease exhibit conformational differences in solution
    • Fabian H, Huser H, Narzi D, Misselwitz R, Loll B, et al. (2008) HLA-B27 subtypes differentially associated with disease exhibit conformational differences in solution. J Mol Biol 376: 798-810.
    • (2008) J Mol Biol , vol.376 , pp. 798-810
    • Fabian, H.1    Huser, H.2    Narzi, D.3    Misselwitz, R.4    Loll, B.5
  • 27
    • 77950531623 scopus 로고    scopus 로고
    • HLA-B27 heavy chains distinguished by a micropolymorphism exhibit differential flexibility
    • Fabian H, Huser H, Loll B, Ziegler A, Naumann D, et al. (2010) HLA-B27 heavy chains distinguished by a micropolymorphism exhibit differential flexibility. Arthritis Rheum 62: 978-987.
    • (2010) Arthritis Rheum , vol.62 , pp. 978-987
    • Fabian, H.1    Huser, H.2    Loll, B.3    Ziegler, A.4    Naumann, D.5
  • 28
    • 24744457740 scopus 로고    scopus 로고
    • CTL recognition of a bulged viral peptide involves biased TCR selection
    • Miles JJ, Elhassen D, Borg NA, Silins SL, Tynan FE, et al. (2005) CTL recognition of a bulged viral peptide involves biased TCR selection. J Immunol 175: 3826-3834.
    • (2005) J Immunol , vol.175 , pp. 3826-3834
    • Miles, J.J.1    Elhassen, D.2    Borg, N.A.3    Silins, S.L.4    Tynan, F.E.5
  • 29
    • 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, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, et al. (2007) A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Nat Immunol 8: 268-276.
    • (2007) Nat Immunol , vol.8 , pp. 268-276
    • Tynan, F.E.1    Reid, H.H.2    Kjer-Nielsen, L.3    Miles, J.J.4    Wilce, M.C.5
  • 30
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-a 60-year-old hypothesis revisited
    • James LC, Tawfik DS, (2003) Conformational diversity and protein evolution-a 60-year-old hypothesis revisited. Trends Biochem Sci 28: 361-368.
    • (2003) Trends Biochem Sci , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 31
    • 38949100462 scopus 로고    scopus 로고
    • The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain
    • Ishizuka J, Stewart-Jones GB, van der Merwe A, Bell JI, McMichael AJ, et al. (2008) The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain. Immunity 28: 171-182.
    • (2008) Immunity , vol.28 , pp. 171-182
    • Ishizuka, J.1    Stewart-Jones, G.B.2    van der Merwe, A.3    Bell, J.I.4    McMichael, A.J.5
  • 32
    • 0025047629 scopus 로고
    • A mutant T4 lysozyme displays five different crystal conformations
    • Faber HR, Matthews BW, (1990) A mutant T4 lysozyme displays five different crystal conformations. Nature 348: 263-266.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 33
    • 0024791087 scopus 로고
    • Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms
    • Ely KR, Herron JN, Harker M, Edmundson AB, (1989) Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms. J Mol Biol 210: 601-615.
    • (1989) J Mol Biol , vol.210 , pp. 601-615
    • Ely, K.R.1    Herron, J.N.2    Harker, M.3    Edmundson, A.B.4
  • 34
  • 35
    • 0026740792 scopus 로고
    • Structural effects induced by mutagenesis affected by crystal packing factors: the structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor
    • Eigenbrot C, Randal M, Kossiakoff AA, (1992) Structural effects induced by mutagenesis affected by crystal packing factors: the structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor. Proteins 14: 75-87.
    • (1992) Proteins , vol.14 , pp. 75-87
    • Eigenbrot, C.1    Randal, M.2    Kossiakoff, A.A.3
  • 37
    • 0025037796 scopus 로고
    • Comparison of the dynamics of myoglobin in different crystal forms
    • Phillips GN Jr, (1990) Comparison of the dynamics of myoglobin in different crystal forms. Biophys J 57: 381-383.
    • (1990) Biophys J , vol.57 , pp. 381-383
    • Phillips Jr., G.N.1
  • 39
    • 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, (1999) Thermodynamics of T cell receptor binding to peptide-MHC: evidence for a general mechanism of molecular scanning. Proc Natl Acad Sci U S A 96: 11446-11451.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11446-11451
    • Boniface, J.J.1    Reich, Z.2    Lyons, D.S.3    Davis, M.M.4
  • 40
    • 77953742968 scopus 로고    scopus 로고
    • Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability
    • Burrows SR, Chen Z, Archbold JK, Tynan FE, Beddoe T, et al. (2010) Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability. Proc Natl Acad Sci U S A 107: 10608-10613.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 10608-10613
    • Burrows, S.R.1    Chen, Z.2    Archbold, J.K.3    Tynan, F.E.4    Beddoe, T.5
  • 41
    • 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, Huseby E, Scott-Browne J, Rubtsova K, Pinilla C, et al. (2011) A single T cell receptor bound to major histocompatibility complex class I and class II glycoproteins reveals switchable TCR conformers. Immunity 35: 23-33.
    • (2011) Immunity , vol.35 , pp. 23-33
    • Yin, L.1    Huseby, E.2    Scott-Browne, J.3    Rubtsova, K.4    Pinilla, C.5
  • 42
    • 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, et al. (2011) Dynamical Characterization of Two Differentially Disease Associated MHC Class I Proteins in Complex with Viral and Self-Peptides. J Mol Biol.
    • (2011) J Mol Biol
    • Narzi, D.1    Becker, C.M.2    Fiorillo, M.T.3    Uchanska-Ziegler, B.4    Ziegler, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.