메뉴 건너뛰기




Volumn 6, Issue 2, 2011, Pages

Understanding TR binding to pMHC complexes: How does a TR scan many pMHC complexes yet preferentially bind to one

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; EPITOPE; LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN; T LYMPHOCYTE RECEPTOR; HLA ANTIGEN CLASS 1; LYMPHOCYTE ANTIGEN RECEPTOR; MULTIPROTEIN COMPLEX;

EID: 79952045349     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017194     Document Type: Article
Times cited : (10)

References (60)
  • 1
    • 74049160009 scopus 로고    scopus 로고
    • Mechanisms maintaining peripheral tolerance
    • Mueller DL, (2010) Mechanisms maintaining peripheral tolerance. Nat Immunol 11: 21-27.
    • (2010) Nat Immunol , vol.11 , pp. 21-27
    • Mueller, D.L.1
  • 2
    • 70350439671 scopus 로고    scopus 로고
    • An endogenous peptide positively selects and augments the activation and survival of peripheral CD4+ T cells
    • Lo WL, Felix NJ, Walters JJ, Rohrs H, Gross ML, et al. (2009) An endogenous peptide positively selects and augments the activation and survival of peripheral CD4+ T cells. Nat Immunol 10: 1155-1161.
    • (2009) Nat Immunol , vol.10 , pp. 1155-1161
    • Lo, W.L.1    Felix, N.J.2    Walters, J.J.3    Rohrs, H.4    Gross, M.L.5
  • 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, et al. (1996) Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 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
  • 4
    • 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, (2009) The molecular basis of TCR germline bias for MHC is surprisingly simple. Nat Immunol 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
  • 5
    • 0003958960 scopus 로고    scopus 로고
    • The T cell receptor FactsBook
    • San Diego, Academic Press
    • Lefranc MP, Lefranc G, (2001) The T cell receptor FactsBook. San Diego Academic Press.
    • (2001)
    • Lefranc, M.P.1    Lefranc, G.2
  • 6
    • 21444450056 scopus 로고    scopus 로고
    • IMGT unique numbering for MHC groove G-DOMAIN and MHC superfamily (MhcSF) G-LIKE-DOMAIN
    • Lefranc MP, Duprat E, Kaas Q, Tranne M, Thiriot A, et al. (2005) IMGT unique numbering for MHC groove G-DOMAIN and MHC superfamily (MhcSF) G-LIKE-DOMAIN. Dev Comp Immunol 29: 917-938.
    • (2005) Dev Comp Immunol , vol.29 , pp. 917-938
    • Lefranc, M.P.1    Duprat, E.2    Kaas, Q.3    Tranne, M.4    Thiriot, A.5
  • 7
    • 2942740952 scopus 로고    scopus 로고
    • The somatic generation of immune recognition. 1971
    • Jerne NK, (2004) The somatic generation of immune recognition. 1971. Eur J Immunol 34: 1234-1242.
    • (2004) Eur J Immunol , vol.34 , pp. 1234-1242
    • Jerne, N.K.1
  • 8
    • 77957258599 scopus 로고    scopus 로고
    • pDOCK: a new technique for rapid and accurate docking of peptide ligands to Major Histocompatibility Complexes
    • Khan JM, Ranganathan S, (2010) pDOCK: a new technique for rapid and accurate docking of peptide ligands to Major Histocompatibility Complexes. Immunome Res 6 (Suppl 1): S2.
    • (2010) Immunome Res , vol.6 , Issue.SUPPL. 1
    • Khan, J.M.1    Ranganathan, S.2
  • 10
    • 0347755625 scopus 로고    scopus 로고
    • IMGT/3Dstructure-DB and IMGT/StructuralQuery, a database and a tool for immunoglobulin, T cell receptor and MHC structural data
    • Kaas Q, Ruiz M, Lefranc MP, (2004) IMGT/3Dstructure-DB and IMGT/StructuralQuery, a database and a tool for immunoglobulin, T cell receptor and MHC structural data. Nucleic Acids Res 32: D208-210.
    • (2004) Nucleic Acids Res , vol.32
    • Kaas, Q.1    Ruiz, M.2    Lefranc, M.P.3
  • 11
    • 75549091258 scopus 로고    scopus 로고
    • IMGT/3Dstructure-DB and IMGT/DomainGapAlign: a database and a tool for immunoglobulins or antibodies, T cell receptors, MHC, IgSF and MhcSF
    • Ehrenmann F, Kaas Q, Lefranc MP, (2010) IMGT/3Dstructure-DB and IMGT/DomainGapAlign: a database and a tool for immunoglobulins or antibodies, T cell receptors, MHC, IgSF and MhcSF. Nucleic Acids Res 38: D301-307.
    • (2010) Nucleic Acids Res , vol.38
    • Ehrenmann, F.1    Kaas, Q.2    Lefranc, M.P.3
  • 12
    • 47649130715 scopus 로고    scopus 로고
    • Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities
    • Armstrong KM, Insaidoo FK, Baker BM, (2008) Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities. J Mol Recognit 21: 275-287.
    • (2008) J Mol Recognit , vol.21 , pp. 275-287
    • Armstrong, K.M.1    Insaidoo, F.K.2    Baker, B.M.3
  • 13
    • 19944430890 scopus 로고    scopus 로고
    • A major histocompatibility complex-peptide-restricted antibody and t cell receptor molecules recognize their target by distinct binding modes: crystal structure of human leukocyte antigen (HLA)-A1-MAGE-A1 in complex with FAB-HYB3
    • Hulsmeyer M, Chames P, Hillig RC, Stanfield RL, Held G, et al. (2005) A major histocompatibility complex-peptide-restricted antibody and t cell receptor molecules recognize their target by distinct binding modes: crystal structure of human leukocyte antigen (HLA)-A1-MAGE-A1 in complex with FAB-HYB3. J Biol Chem 280: 2972-2980.
    • (2005) J Biol Chem , vol.280 , pp. 2972-2980
    • Hulsmeyer, M.1    Chames, P.2    Hillig, R.C.3    Stanfield, R.L.4    Held, G.5
  • 14
    • 5944249467 scopus 로고    scopus 로고
    • Crystal structure of a T cell receptor bound to an allogeneic MHC molecule
    • Reiser JB, Darnault C, Guimezanes A, Gregoire C, Mosser T, et al. (2000) Crystal structure of a T cell receptor bound to an allogeneic MHC molecule. Nat Immunol 1: 291-297.
    • (2000) Nat Immunol , vol.1 , pp. 291-297
    • Reiser, J.B.1    Darnault, C.2    Guimezanes, A.3    Gregoire, C.4    Mosser, T.5
  • 16
    • 0034329441 scopus 로고    scopus 로고
    • Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
    • Hennecke J, Carfi A, Wiley DC, (2000) Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1. EMBO J 19: 5611-5624.
    • (2000) EMBO J , vol.19 , pp. 5611-5624
    • Hennecke, J.1    Carfi, A.2    Wiley, D.C.3
  • 18
    • 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, (1999) Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity 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
  • 19
    • 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, et al. (2005) 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 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
  • 20
    • 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, Langley RJ, Brown PH, Xu G, Teng L, et al. (2007) Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor. Nat Immunol 8: 398-408.
    • (2007) Nat Immunol , vol.8 , pp. 398-408
    • Deng, L.1    Langley, R.J.2    Brown, P.H.3    Xu, G.4    Teng, L.5
  • 23
    • 34548826509 scopus 로고    scopus 로고
    • Single MHC mutation eliminates enthalpy associated with T cell receptor binding
    • Miller PJ, Pazy Y, Conti B, Riddle D, Appella E, et al. (2007) Single MHC mutation eliminates enthalpy associated with T cell receptor binding. J Mol Biol 373: 315-327.
    • (2007) J Mol Biol , vol.373 , pp. 315-327
    • Miller, P.J.1    Pazy, Y.2    Conti, B.3    Riddle, D.4    Appella, E.5
  • 25
    • 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
  • 26
    • 20944450033 scopus 로고    scopus 로고
    • Structural and kinetic basis for heightened immunogenicity of T cell vaccines
    • Chen JL, Stewart-Jones G, Bossi G, Lissin NM, Wooldridge L, et al. (2005) Structural and kinetic basis for heightened immunogenicity of T cell vaccines. J Exp Med 201: 1243-1255.
    • (2005) J Exp Med , vol.201 , pp. 1243-1255
    • Chen, J.L.1    Stewart-Jones, G.2    Bossi, G.3    Lissin, N.M.4    Wooldridge, L.5
  • 27
    • 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
  • 28
    • 34247346627 scopus 로고    scopus 로고
    • How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?
    • Mazza C, Auphan-Anezin N, Gregoire C, Guimezanes A, Kellenberger C, et al. (2007) How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides? EMBO J 26: 1972-1983.
    • (2007) EMBO J , vol.26 , pp. 1972-1983
    • Mazza, C.1    Auphan-Anezin, N.2    Gregoire, C.3    Guimezanes, A.4    Kellenberger, C.5
  • 29
    • 77951817966 scopus 로고    scopus 로고
    • The diabetogenic mouse MHC class II molecule I-Ag7 is endowed with a switch that modulates TCR affinity
    • Yoshida K, Corper AL, Herro R, Jabri B, Wilson IA, et al. (2010) The diabetogenic mouse MHC class II molecule I-Ag7 is endowed with a switch that modulates TCR affinity. J Clin Invest 120: 1578-1590.
    • (2010) J Clin Invest , vol.120 , pp. 1578-1590
    • Yoshida, K.1    Corper, A.L.2    Herro, R.3    Jabri, B.4    Wilson, I.A.5
  • 30
    • 0033046472 scopus 로고    scopus 로고
    • Immunodominance in major histocompatibility complex class I-restricted T lymphocyte responses
    • Yewdell JW, Bennink JR, (1999) Immunodominance in major histocompatibility complex class I-restricted T lymphocyte responses. Annu Rev Immunol 17: 51-88.
    • (1999) Annu Rev Immunol , vol.17 , pp. 51-88
    • Yewdell, J.W.1    Bennink, J.R.2
  • 31
    • 32544458887 scopus 로고    scopus 로고
    • T cell receptor/peptide/MHC molecular characterization and standardized pMHC contact sites in IMGT/3Dstructure-DB
    • Kaas Q, Lefranc MP, (2005) T cell receptor/peptide/MHC molecular characterization and standardized pMHC contact sites in IMGT/3Dstructure-DB. In Silico Biol 5: 505-528.
    • (2005) In Silico Biol , vol.5 , pp. 505-528
    • Kaas, Q.1    Lefranc, M.P.2
  • 32
    • 46049113012 scopus 로고    scopus 로고
    • IMGT standardization for molecular characterization of the T cell receptor/peptide/MHC complexes
    • In: Schoenbach C, Ranganathan S, Brusic V, editors, New York, Springer
    • Kaas Q, Duprat E, Tourneur G, Lefranc MP, (2008) IMGT standardization for molecular characterization of the T cell receptor/peptide/MHC complexes. In: Schoenbach C, Ranganathan S, Brusic V, editors. Immunoinformatics, Immunomics Reviews Series New York Springer pp. 19-49.
    • (2008) Immunoinformatics, Immunomics Reviews Series , pp. 19-49
    • Kaas, Q.1    Duprat, E.2    Tourneur, G.3    Lefranc, M.P.4
  • 33
    • 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, Gregoire C, Darnault C, Mosser T, Guimezanes A, et al. (2002) A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. Immunity 16: 345-354.
    • (2002) Immunity , vol.16 , pp. 345-354
    • Reiser, J.B.1    Gregoire, C.2    Darnault, C.3    Mosser, T.4    Guimezanes, A.5
  • 34
    • 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, (1997) The MHC reactivity of the T cell repertoire prior to positive and negative selection. Cell 88: 627-636.
    • (1997) Cell , vol.88 , pp. 627-636
    • Zerrahn, J.1    Held, W.2    Raulet, D.H.3
  • 35
    • 0037212339 scopus 로고    scopus 로고
    • IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains
    • Lefranc MP, Pommie C, Ruiz M, Giudicelli V, Foulquier E, et al. (2003) IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains. Dev Comp Immunol 27: 55-77.
    • (2003) Dev Comp Immunol , vol.27 , pp. 55-77
    • Lefranc, M.P.1    Pommie, C.2    Ruiz, M.3    Giudicelli, V.4    Foulquier, E.5
  • 36
    • 0033520962 scopus 로고    scopus 로고
    • The crystal structure of a T cell receptor in complex with peptide and MHC class II
    • Reinherz EL, Tan K, Tang L, Kern P, Liu J, et al. (1999) The crystal structure of a T cell receptor in complex with peptide and MHC class II. Science 286: 1913-1921.
    • (1999) Science , vol.286 , pp. 1913-1921
    • Reinherz, E.L.1    Tan, K.2    Tang, L.3    Kern, P.4    Liu, J.5
  • 37
    • 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, et al. (1998) Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity 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
  • 38
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia KC, Degano M, Pease LR, Huang M, Peterson PA, et al. (1998) Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279: 1166-1172.
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1    Degano, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5
  • 39
    • 0033520991 scopus 로고    scopus 로고
    • Perspectives: protein structure. Class-conscious TCR?
    • Wilson IA, (1999) Perspectives: protein structure. Class-conscious TCR? Science 286: 1867-1868.
    • (1999) Science , vol.286 , pp. 1867-1868
    • Wilson, I.A.1
  • 40
    • 0037240790 scopus 로고    scopus 로고
    • A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity
    • Kjer-Nielsen L, Clements CS, Purcell AW, Brooks AG, Whisstock JC, et al. (2003) A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity. Immunity 18: 53-64.
    • (2003) Immunity , vol.18 , pp. 53-64
    • Kjer-Nielsen, L.1    Clements, C.S.2    Purcell, A.W.3    Brooks, A.G.4    Whisstock, J.C.5
  • 41
    • 0037018102 scopus 로고    scopus 로고
    • Structure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivity
    • Hennecke J, Wiley DC, (2002) Structure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivity. J Exp Med 195: 571-581.
    • (2002) J Exp Med , vol.195 , pp. 571-581
    • Hennecke, J.1    Wiley, D.C.2
  • 42
    • 12344322695 scopus 로고    scopus 로고
    • High-affinity, peptide-specific T cell receptors can be generated by mutations in CDR1, CDR2 or CDR3
    • Chlewicki LK, Holler PD, Monti BC, Clutter MR, Kranz DM, (2005) High-affinity, peptide-specific T cell receptors can be generated by mutations in CDR1, CDR2 or CDR3. J Mol Biol 346: 223-239.
    • (2005) J Mol Biol , vol.346 , pp. 223-239
    • Chlewicki, L.K.1    Holler, P.D.2    Monti, B.C.3    Clutter, M.R.4    Kranz, D.M.5
  • 43
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • McCoy AJ, Chandana Epa V, Colman PM, (1997) Electrostatic complementarity at protein/protein interfaces. J Mol Biol 268: 570-584.
    • (1997) J Mol Biol , vol.268 , pp. 570-584
    • McCoy, A.J.1    Chandana Epa, V.2    Colman, P.M.3
  • 44
    • 18244392426 scopus 로고    scopus 로고
    • Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor
    • 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.
    • (2005) Nat Immunol , vol.6 , pp. 490-496
    • Hahn, M.1    Nicholson, M.J.2    Pyrdol, J.3    Wucherpfennig, K.W.4
  • 46
    • 0142219443 scopus 로고    scopus 로고
    • A correlation between TCR Valpha docking on MHC and CD8 dependence: implications for T cell selection
    • 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.
    • (2003) Immunity , vol.19 , pp. 595-606
    • Buslepp, J.1    Wang, H.2    Biddison, W.E.3    Appella, E.4    Collins, E.J.5
  • 48
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG, (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 49
    • 0030305457 scopus 로고    scopus 로고
    • R: A language for data analysis and graphics
    • Ihaka R, Gentleman R, (1996) R: A language for data analysis and graphics. J Comput and Graph Stat 5: 299-314.
    • (1996) J Comput and Graph Stat , vol.5 , pp. 299-314
    • Ihaka, R.1    Gentleman, R.2
  • 50
    • 33645498495 scopus 로고    scopus 로고
    • Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity
    • Dunn SM, Rizkallah PJ, Baston E, Mahon T, Cameron B, et al. (2006) Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity. Protein Sci 15: 710-721.
    • (2006) Protein Sci , vol.15 , pp. 710-721
    • Dunn, S.M.1    Rizkallah, P.J.2    Baston, E.3    Mahon, T.4    Cameron, B.5
  • 51
    • 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
  • 52
    • 60549093248 scopus 로고    scopus 로고
    • Natural micropolymorphism in human leukocyte antigens provides a basis for genetic control of antigen recognition
    • Archbold JK, Macdonald WA, Gras S, Ely LK, Miles JJ, et al. (2009) Natural micropolymorphism in human leukocyte antigens provides a basis for genetic control of antigen recognition. J Exp Med 206: 209-219.
    • (2009) J Exp Med , vol.206 , pp. 209-219
    • Archbold, J.K.1    Macdonald, W.A.2    Gras, S.3    Ely, L.K.4    Miles, J.J.5
  • 54
    • 33846977011 scopus 로고    scopus 로고
    • Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC
    • Wang L, Zhao Y, Li Z, Guo Y, Jones LL, et al. (2007) Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. Nat Struct Mol Biol 14: 169-171.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 169-171
    • Wang, L.1    Zhao, Y.2    Li, Z.3    Guo, Y.4    Jones, L.L.5
  • 55
    • 10644239910 scopus 로고    scopus 로고
    • T cell cross-reactivity and conformational changes during TCR engagement
    • Lee JK, Stewart-Jones G, Dong T, Harlos K, Di Gleria K, et al. (2004) T cell cross-reactivity and conformational changes during TCR engagement. J Exp Med 200: 1455-1466.
    • (2004) J Exp Med , vol.200 , pp. 1455-1466
    • Lee, J.K.1    Stewart-Jones, G.2    Dong, T.3    Harlos, K.4    Di Gleria, K.5
  • 56
    • 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
  • 57
    • 2642524483 scopus 로고    scopus 로고
    • A physical reference state unifies the structure-derived potential of mean force for protein folding and binding
    • Liu S, Zhang C, Zhou H, Zhou Y, (2004) A physical reference state unifies the structure-derived potential of mean force for protein folding and binding. Proteins 56: 93-101.
    • (2004) Proteins , vol.56 , pp. 93-101
    • Liu, S.1    Zhang, C.2    Zhou, H.3    Zhou, Y.4
  • 58
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou H, Zhou Y, (2002) Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci 11: 2714-2726.
    • (2002) Protein Sci , vol.11 , pp. 2714-2726
    • Zhou, H.1    Zhou, Y.2
  • 59
    • 84986522918 scopus 로고
    • ICM: A new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation
    • Abagyan RA, Totrov MM, Kuznetsov DA, (1994) ICM: A new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J Comp Chem 15: 488-506.
    • (1994) J Comp Chem , vol.15 , pp. 488-506
    • Abagyan, R.A.1    Totrov, M.M.2    Kuznetsov, D.A.3
  • 60
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan RA, Totrov MM, (1994) Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J Mol Biol 235: 983-1002.
    • (1994) J Mol Biol , vol.235 , pp. 983-1002
    • Abagyan, R.A.1    Totrov, M.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.