메뉴 건너뛰기




Volumn 7, Issue 3, 2012, Pages

Interaction pattern of Arg 62 in the a-pocket of differentially disease-associated HLA-B27 subtypes suggests distinct TCR binding modes

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; COMPLEMENTARY DNA; EPIDERMAL GROWTH FACTOR; HLA B27 ANTIGEN; INFLUENZA A VIRUS NUCLEOPROTEIN; LATENT MEMBRANE PROTEIN 2; LYSINE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1; VIRUS NUCLEOPROTEIN; HLA B*27:05 ANTIGEN; HLA B*27:09 ANTIGEN; HLA-B*27:05 ANTIGEN; HLA-B*27:09 ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; OLIGOPEPTIDE; SOLVENT;

EID: 84857759560     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0032865     Document Type: Article
Times cited : (17)

References (64)
  • 1
    • 33846117141 scopus 로고    scopus 로고
    • Plumbing the sources of endogenous MHC class I peptide ligands
    • Yedwell JW, (2007) Plumbing the sources of endogenous MHC class I peptide ligands. Curr Opin Immunol 19: 79-86.
    • (2007) Curr Opin Immunol , vol.19 , pp. 79-86
    • Yedwell, J.W.1
  • 2
    • 0025813156 scopus 로고
    • The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
    • Madden DR, Gorga JC, Strominger JL, Wiley DC, (1991) The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature 353: 321-325.
    • (1991) Nature , vol.353 , pp. 321-325
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 3
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden DR, Gorga JC, Strominger JL, Wiley DC, (1992) The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell 70: 1035-1048.
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 4
    • 77955232539 scopus 로고    scopus 로고
    • Structure and function of major histocompatibility complex class I antigens
    • Li XC, Raghavan M, (2010) Structure and function of major histocompatibility complex class I antigens. Curr Opin Organ Transplant 15: 499-504.
    • (2010) Curr Opin Organ Transplant , vol.15 , pp. 499-504
    • Li, X.C.1    Raghavan, M.2
  • 8
    • 3142543331 scopus 로고    scopus 로고
    • Differential peptide dynamics is linked to major histocompatibility complex polymorphism
    • Pöhlmann T, Böckmann RA, Grubmüller 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
    • Pöhlmann, T.1    Böckmann, R.A.2    Grubmüller, H.3    Uchanska-Ziegler, B.4    Ziegler, A.5
  • 9
    • 45849131354 scopus 로고    scopus 로고
    • Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
    • Lange OF, Lakomek NA, Fares C, Schröder GF, Walter KFA, et al. (2008) Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science 320: 1471-1475.
    • (2008) Science , vol.320 , pp. 1471-1475
    • Lange, O.F.1    Lakomek, N.A.2    Fares, C.3    Schröder, G.F.4    Walter, K.F.A.5
  • 10
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland DE, (1958) Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci USA 44: 98-104.
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 12
    • 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 USA 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
  • 14
    • 0015914854 scopus 로고
    • High association of an HL-A antigen, W27, with ankylosing spondylitis
    • Schlosstein L, Terasaki PI, Bluestone R, Pearson CM, (1973) High association of an HL-A antigen, W27, with ankylosing spondylitis. N Engl J Med 288: 704-706.
    • (1973) N Engl J Med , vol.288 , pp. 704-706
    • Schlosstein, L.1    Terasaki, P.I.2    Bluestone, R.3    Pearson, C.M.4
  • 15
    • 0027274825 scopus 로고
    • Conservation of T cell receptor usage by HLA B27-restricted influenza-specific cytotoxic T lymphocytes suggests a general pattern for antigen-specific major histocompatibility complex class I-restricted responses
    • Bowness P, Moss PA, Rowland-Jones S, Bell JI, McMichael AJ, (1993) Conservation of T cell receptor usage by HLA B27-restricted influenza-specific cytotoxic T lymphocytes suggests a general pattern for antigen-specific major histocompatibility complex class I-restricted responses. Eur J Immunol 23: 1417-1421.
    • (1993) Eur J Immunol , vol.23 , pp. 1417-1421
    • Bowness, P.1    Moss, P.A.2    Rowland-Jones, S.3    Bell, J.I.4    McMichael, A.J.5
  • 16
    • 0027261331 scopus 로고
    • Different HLA-B27 subtypes present the same immunodominant Epstein-Barr virus peptide
    • Brooks JM, Murray RJ, Thomas WA, Kurilla MG, Rickinson AB, (1993) Different HLA-B27 subtypes present the same immunodominant Epstein-Barr virus peptide. J Exp Med 178: 879-887.
    • (1993) J Exp Med , vol.178 , pp. 879-887
    • Brooks, J.M.1    Murray, R.J.2    Thomas, W.A.3    Kurilla, M.G.4    Rickinson, A.B.5
  • 17
    • 33645229492 scopus 로고    scopus 로고
    • Dominant influence of an HLA-B27 restricted CD8+ T cell response in mediating HCV clearance and evolution
    • Neumann-Haefelin C, McKiernan S, Ward S, Viazov S, Spangenberg HC, et al. (2006) Dominant influence of an HLA-B27 restricted CD8+ T cell response in mediating HCV clearance and evolution. Hepatology 43: 563-572.
    • (2006) Hepatology , vol.43 , pp. 563-572
    • Neumann-Haefelin, C.1    McKiernan, S.2    Ward, S.3    Viazov, S.4    Spangenberg, H.C.5
  • 18
    • 0001426414 scopus 로고    scopus 로고
    • Direct visualization of HIV-1-specific cytotoxic T lymphocytes during primary infection
    • Wilson JD, Ogg GS, Allen RL, Davis C, Shaunak S, et al. (2000) Direct visualization of HIV-1-specific cytotoxic T lymphocytes during primary infection. AIDS 14: 225-233.
    • (2000) AIDS , vol.14 , pp. 225-233
    • Wilson, J.D.1    Ogg, G.S.2    Allen, R.L.3    Davis, C.4    Shaunak, S.5
  • 21
    • 70349580108 scopus 로고    scopus 로고
    • Subtypes of HLA-B27: history and implications in the pathogenesis of ankylosing spondylitis
    • Reveille JD, Maganti RM, (2009) Subtypes of HLA-B27: history and implications in the pathogenesis of ankylosing spondylitis. Adv Exp Med Biol 649: 159-176.
    • (2009) Adv Exp Med Biol , vol.649 , pp. 159-176
    • Reveille, J.D.1    Maganti, R.M.2
  • 22
    • 26844522808 scopus 로고    scopus 로고
    • Distribution of HLA-B27 subtypes in Sardinia and continental Italy and their association with spondylarthropathies
    • Paladini F, Taccari E, Fiorillo MT, Cauli A, Passiu G, et al. (2005) Distribution of HLA-B27 subtypes in Sardinia and continental Italy and their association with spondylarthropathies. Arthritis Rheum 52: 3319-3321.
    • (2005) Arthritis Rheum , vol.52 , pp. 3319-3321
    • Paladini, F.1    Taccari, E.2    Fiorillo, M.T.3    Cauli, A.4    Passiu, G.5
  • 23
    • 0028022808 scopus 로고
    • Identification of a novel HLA-B27 subtype by restriction analysis of a cytotoxic γδ T cell clone
    • Del Porto P, D'Amato M, Fiorillo MT, Tuosto L, Piccolella E, et al. (1994) Identification of a novel HLA-B27 subtype by restriction analysis of a cytotoxic γδ T cell clone. J Immunol 153: 3093-3100.
    • (1994) J Immunol , vol.153 , pp. 3093-3100
    • Del Porto, P.1    D'Amato, M.2    Fiorillo, M.T.3    Tuosto, L.4    Piccolella, E.5
  • 24
    • 0031051908 scopus 로고    scopus 로고
    • Susceptibility to ankylosing spondylitis correlates with the C-terminal residue of peptides presented by various HLA-B27 subtypes
    • Fiorillo MT, Meadows L, D'Amato M, Shabanowitz J, Hunt DE, et al. (1997) Susceptibility to ankylosing spondylitis correlates with the C-terminal residue of peptides presented by various HLA-B27 subtypes. Eur J Immunol 27: 368-373.
    • (1997) Eur J Immunol , vol.27 , pp. 368-373
    • Fiorillo, M.T.1    Meadows, L.2    D'Amato, M.3    Shabanowitz, J.4    Hunt, D.E.5
  • 25
    • 0031903713 scopus 로고    scopus 로고
    • The naturally occurring polymorphism Asp116-His116 differentiating the ankylosing spondylitis associated HLA-B*2705 from the non-associated HLA-B*2709 subtype influences peptide-specific CD8 T cells recognition
    • Fiorillo MT, Greco G, Maragno M, Potolicchio I, Monizio A, et al. (1998) The naturally occurring polymorphism Asp116-His116 differentiating the ankylosing spondylitis associated HLA-B*2705 from the non-associated HLA-B*2709 subtype influences peptide-specific CD8 T cells recognition. Eur J Immunol 28: 2508-2516.
    • (1998) Eur J Immunol , vol.28 , pp. 2508-2516
    • Fiorillo, M.T.1    Greco, G.2    Maragno, M.3    Potolicchio, I.4    Monizio, A.5
  • 26
    • 0033935853 scopus 로고    scopus 로고
    • CD8+ T cell autoreactivity to an HLA-B27-restricted self-epitope correlates with ankylosing spondylitis
    • Fiorillo, MT, Maragno M, Butler R, Dupuis ML, Sorrentino R, (2000) CD8+ T cell autoreactivity to an HLA-B27-restricted self-epitope correlates with ankylosing spondylitis. J Clin Invest 106: 47-53.
    • (2000) J Clin Invest , vol.106 , pp. 47-53
    • Fiorillo, M.T.1    Maragno, M.2    Butler, R.3    Dupuis, M.L.4    Sorrentino, R.5
  • 27
    • 70349575011 scopus 로고    scopus 로고
    • T cell responses against viral and self-epitopes and HLA-B27 subtypes differently associated with Ankylosing Spondylitis
    • Fiorillo MT, Sorrentino R, (2009) T cell responses against viral and self-epitopes and HLA-B27 subtypes differently associated with Ankylosing Spondylitis. Adv Exp Med Biol 649: 255-262.
    • (2009) Adv Exp Med Biol , vol.649 , pp. 255-262
    • Fiorillo, M.T.1    Sorrentino, R.2
  • 29
    • 13244249798 scopus 로고    scopus 로고
    • Allele-dependent similarity between viral and self-peptide presentation by HLA-B27 subtypes
    • Fiorillo MT, Ruckert C, Hulsmeyer M, Sorrentino R, Saenger W, et al. (2005) Allele-dependent similarity between viral and self-peptide presentation by HLA-B27 subtypes. J Biol Chem 280: 2962-2971.
    • (2005) J Biol Chem , vol.280 , pp. 2962-2971
    • Fiorillo, M.T.1    Ruckert, C.2    Hulsmeyer, M.3    Sorrentino, R.4    Saenger, W.5
  • 31
    • 9144262462 scopus 로고    scopus 로고
    • Thermodynamic and structural analysis of peptide- and allele-dependent properties of two HLA-B27 subtypes exhibiting differential disease association
    • Hillig RC, Hulsmeyer M, Saenger W, Welfle K, Misselwitz R, et al. (2004) Thermodynamic and structural analysis of peptide- and allele-dependent properties of two HLA-B27 subtypes exhibiting differential disease association. J Biol Chem 279: 652-666.
    • (2004) J Biol Chem , vol.279 , pp. 652-666
    • Hillig, R.C.1    Hulsmeyer, M.2    Saenger, W.3    Welfle, K.4    Misselwitz, R.5
  • 32
    • 13844276058 scopus 로고    scopus 로고
    • Thermodynamic and structural equivalence of two HLA-B27 subtypes complexed with a self-peptide
    • Hülsmeyer M, Welfle K, Pöhlmann T, Misselwitz R, Alexiev U, et al. (2005) Thermodynamic and structural equivalence of two HLA-B27 subtypes complexed with a self-peptide. J Mol Biol 346: 1367-1379.
    • (2005) J Mol Biol , vol.346 , pp. 1367-1379
    • Hülsmeyer, M.1    Welfle, K.2    Pöhlmann, T.3    Misselwitz, R.4    Alexiev, U.5
  • 33
    • 18344394144 scopus 로고    scopus 로고
    • A T cell receptor CDR3β loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex
    • Reiser JB, Grégoire C, Darnault C, Mosser T, Guimezanes A, et al. (2002) A T cell receptor CDR3β loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. Immunity 216: 345-354.
    • (2002) Immunity , vol.216 , pp. 345-354
    • Reiser, J.B.1    Grégoire, C.2    Darnault, C.3    Mosser, T.4    Guimezanes, A.5
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0025048105 scopus 로고
    • Molecular-Dynamics simulations in biology
    • Karplus M, Petsko GA, (1990) Molecular-Dynamics simulations in biology. Nature 347: 631-639.
    • (1990) Nature , vol.347 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 37
    • 0028135684 scopus 로고
    • Molecular Dynamics simulation of MHC-Peptide complexes as a tool for predicting potential T Cell epitopes
    • Rognan D, Scapozza L, Folkers G, Daser A, (1994) Molecular Dynamics simulation of MHC-Peptide complexes as a tool for predicting potential T Cell epitopes. Biochemistry 33: 11476-11485.
    • (1994) Biochemistry , vol.33 , pp. 11476-11485
    • Rognan, D.1    Scapozza, L.2    Folkers, G.3    Daser, A.4
  • 38
    • 0031226806 scopus 로고    scopus 로고
    • Fine specificity of antigen binding to two class I major histocompatibility proteins (B*2705 and B*2703) differing in a single amino acid residue
    • Rognan D, Krebs S, Kuonen O, Lamas JR, Lopez de Castro JA, et al. (1997) Fine specificity of antigen binding to two class I major histocompatibility proteins (B*2705 and B*2703) differing in a single amino acid residue. J Comput Aided Mol Des 11: 463-478.
    • (1997) J Comput Aided Mol Des , vol.11 , pp. 463-478
    • Rognan, D.1    Krebs, S.2    Kuonen, O.3    Lamas, J.R.4    de Castro, J.A.L.5
  • 39
    • 33846550599 scopus 로고    scopus 로고
    • Comparative molecular dynamics analysis of tapasin-dependent and -independent MHC class I alleles
    • Sieker F, Springer S, Zacharias M, (2007) Comparative molecular dynamics analysis of tapasin-dependent and-independent MHC class I alleles. Protein Sci 16: 299-308.
    • (2007) Protein Sci , vol.16 , pp. 299-308
    • Sieker, F.1    Springer, S.2    Zacharias, M.3
  • 40
    • 48049122834 scopus 로고    scopus 로고
    • Differential tapasin dependence of MHC class I molecules correlates with conformational changes upon peptide dissociation: A molecular dynamics simulation study
    • Sieker F, Straatsma TP, Springer S, Zacharias M, (2008) Differential tapasin dependence of MHC class I molecules correlates with conformational changes upon peptide dissociation: A molecular dynamics simulation study. Mol Immunol 45: 3714-3722.
    • (2008) Mol Immunol , vol.45 , pp. 3714-3722
    • Sieker, F.1    Straatsma, T.P.2    Springer, S.3    Zacharias, M.4
  • 41
    • 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
  • 42
    • 49649086640 scopus 로고    scopus 로고
    • Analysis of key parameters for molecular dynamics of pMHC molecules
    • Omasits U, Knapp B, Neumann M, Steinhauser O, Stockinger H, et al. (2008) Analysis of key parameters for molecular dynamics of pMHC molecules. Mol Simul 34: 781-793.
    • (2008) Mol Simul , vol.34 , pp. 781-793
    • Omasits, U.1    Knapp, B.2    Neumann, M.3    Steinhauser, O.4    Stockinger, H.5
  • 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, et al. (2012) Dynamical characterization of two differentially disease associated MHC Class I proteins in complex with viral- and self-peptides. J Mol Biol 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
  • 44
    • 70349567381 scopus 로고    scopus 로고
    • Implications of structural and thermodynamic studies of HLA-B27 subtypes exhibiting differential association with ankylosing spondylitis
    • Ziegler A, Loll B, Misselwitz R, Uchanska-Ziegler B, (2009) Implications of structural and thermodynamic studies of HLA-B27 subtypes exhibiting differential association with ankylosing spondylitis. Adv Exp Med Biol 649: 177-195.
    • (2009) Adv Exp Med Biol , vol.649 , pp. 177-195
    • Ziegler, A.1    Loll, B.2    Misselwitz, R.3    Uchanska-Ziegler, B.4
  • 45
    • 14744303956 scopus 로고    scopus 로고
    • Crystal structures and KIR3DL1 recognition of three immunodominant viral peptides complexed to HLA-B*2705
    • Stewart-Jones GB, di Gleria K, Kollnberger S, McMichael AJ, Jones EY, et al. (2005) Crystal structures and KIR3DL1 recognition of three immunodominant viral peptides complexed to HLA-B*2705. Eur J Immunol 35: 341-351.
    • (2005) Eur J Immunol , vol.35 , pp. 341-351
    • Stewart-Jones, G.B.1    di Gleria, K.2    Kollnberger, S.3    McMichael, A.J.4    Jones, E.Y.5
  • 46
    • 0028366361 scopus 로고
    • Dominant aromatic/aliphatic C-terminal anchor in HLA-B*2702 and B*2705 peptide motifs
    • Rotzschke O, Falk K, Stefanovic S, Gnau V, Jung G, et al. (1994) Dominant aromatic/aliphatic C-terminal anchor in HLA-B*2702 and B*2705 peptide motifs. Immunogenetics 39: 74-77.
    • (1994) Immunogenetics , vol.39 , pp. 74-77
    • Rotzschke, O.1    Falk, K.2    Stefanovic, S.3    Gnau, V.4    Jung, G.5
  • 47
    • 0037047424 scopus 로고    scopus 로고
    • Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability
    • Ramos M, Paradela A, Vazquez M, Marina A, Vazquez J, et al. (2002) Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability. J Biol Chem 277: 28749-28756.
    • (2002) J Biol Chem , vol.277 , pp. 28749-28756
    • Ramos, M.1    Paradela, A.2    Vazquez, M.3    Marina, A.4    Vazquez, J.5
  • 49
    • 0020300724 scopus 로고
    • Recognition of HLA-B27 and related antigen by a monoclonal antibody
    • Ellis SA, Taylor C, McMichael A, (1982) Recognition of HLA-B27 and related antigen by a monoclonal antibody. Hum Immunol 5: 49-59.
    • (1982) Hum Immunol , vol.5 , pp. 49-59
    • Ellis, S.A.1    Taylor, C.2    McMichael, A.3
  • 50
    • 0022533999 scopus 로고
    • Monoclonal antibodies raised against denaturated HLA-B locus heavy chain permit biochemical characterization of certain HLA-C locus products
    • Stam NJ, Spits H, Ploegh HL, (1986) Monoclonal antibodies raised against denaturated HLA-B locus heavy chain permit biochemical characterization of certain HLA-C locus products. J Immunol 137: 2299-2306.
    • (1986) J Immunol , vol.137 , pp. 2299-2306
    • Stam, N.J.1    Spits, H.2    Ploegh, H.L.3
  • 51
    • 0036839356 scopus 로고    scopus 로고
    • The structure of HLA-B8 complexed to an immunodominant viral determinant: peptide-induced conformational changes and a mode of MHC class I dimerization
    • Kjer-Nielsen L, Clements CS, Brooks AG, Purcell AW, Fontes MR, et al. (2002) The structure of HLA-B8 complexed to an immunodominant viral determinant: peptide-induced conformational changes and a mode of MHC class I dimerization. J Immunol 169: 5153-5160.
    • (2002) J Immunol , vol.169 , pp. 5153-5160
    • Kjer-Nielsen, L.1    Clements, C.S.2    Brooks, A.G.3    Purcell, A.W.4    Fontes, M.R.5
  • 52
  • 53
    • 2942754097 scopus 로고    scopus 로고
    • The structure of H-2K(b) and K(bm8) complexed to a herpes simplex virus determinant: evidence for a conformational switch that governs T cell repertoire selection and viral resistance
    • Webb AI, Borg NA, Dunstone MA, Kjer-Nielsen L, Beddoe T, et al. (2004) The structure of H-2K(b) and K(bm8) complexed to a herpes simplex virus determinant: evidence for a conformational switch that governs T cell repertoire selection and viral resistance. J Immunol 173: 402-409.
    • (2004) J Immunol , vol.173 , pp. 402-409
    • Webb, A.I.1    Borg, N.A.2    Dunstone, M.A.3    Kjer-Nielsen, L.4    Beddoe, T.5
  • 54
    • 59849128475 scopus 로고    scopus 로고
    • Presentation of cytosolically stable peptides by HLA-B27 is not dependent on the canonic interactions of N-terminal basic residues in the A pocket
    • Gomez P, Mavian C, Galocha B, Garcia-Medel N, López de Castro JA, (2009) Presentation of cytosolically stable peptides by HLA-B27 is not dependent on the canonic interactions of N-terminal basic residues in the A pocket. J Immunol 182: 446-455.
    • (2009) J Immunol , vol.182 , pp. 446-455
    • Gomez, P.1    Mavian, C.2    Galocha, B.3    Garcia-Medel, N.4    de Castro, J.A.L.5
  • 55
    • 0028105911 scopus 로고
    • Identification of T cell receptor recognition residues for a viral peptide presented by HLA B27
    • Bowness P, Allen R, McMichael AJ, (1994) Identification of T cell receptor recognition residues for a viral peptide presented by HLA B27. Eur J Immunol 24: 2357-2363.
    • (1994) Eur J Immunol , vol.24 , pp. 2357-2363
    • Bowness, P.1    Allen, R.2    McMichael, A.J.3
  • 56
    • 53149153573 scopus 로고    scopus 로고
    • Molecular determinants of major histocompatibility complex class I complex stability
    • Narzi D, Winkler K, Saidowsky J, Misselwitz R, Ziegler A, et al. (2008) Molecular determinants of major histocompatibility complex class I complex stability. J Biol Chem 283: 23093-23103.
    • (2008) J Biol Chem , vol.283 , pp. 23093-23103
    • Narzi, D.1    Winkler, K.2    Saidowsky, J.3    Misselwitz, R.4    Ziegler, A.5
  • 57
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G, (1990) WHAT IF: A molecular modeling and drug design program. J Mol Graph 8: 52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 58
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 59
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL, (2001) Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J Phys Chem B 105: 6474-6487.
    • (2001) J Phys Chem B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 61
    • 33846823909 scopus 로고
    • Particle mesh Ewald: "An N log(N) method for Ewald sums in large systems"
    • Darden TA, York DM, Pedersen LG, (1993) Particle mesh Ewald: "An N log(N) method for Ewald sums in large systems". J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.M.2    Pedersen, L.G.3
  • 64
    • 77951879368 scopus 로고    scopus 로고
    • CD8+ T-cell mediated self-reactivity in HLA-B27 context as a consequence of dual peptide conformation
    • Nurzia E, Panimolle F, Cauli A, Mathieu A, Magnacca A, et al. (2010) CD8+ T-cell mediated self-reactivity in HLA-B27 context as a consequence of dual peptide conformation. Clin Immunol 135: 476-482.
    • (2010) Clin Immunol , vol.135 , pp. 476-482
    • Nurzia, E.1    Panimolle, F.2    Cauli, A.3    Mathieu, A.4    Magnacca, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.