메뉴 건너뛰기




Volumn 40, Issue 7, 1997, Pages 1316-1326

Use of T cell receptor/HLA-DRB1*04 molecular modeling to predict site- specific interactions for the DR shared epitope associated with rheumatoid arthritis

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; HLA DR ANTIGEN; T LYMPHOCYTE RECEPTOR;

EID: 0030885064     PISSN: 00043591     EISSN: None     Source Type: Journal    
DOI: 10.1002/1529-0131(199707)40:7<1316::AID-ART17>3.0.CO;2-I     Document Type: Article
Times cited : (24)

References (61)
  • 1
    • 0023500817 scopus 로고
    • The shared epitope hypothesis: An approach to understanding the molecular genetics of susceptibility to rheumatoid arthritis
    • Gregersen PK, Silver J, Winchester RJ: The shared epitope hypothesis: an approach to understanding the molecular genetics of susceptibility to rheumatoid arthritis. Arthritis Rheum 30:1205-1213, 1987
    • (1987) Arthritis Rheum , vol.30 , pp. 1205-1213
    • Gregersen, P.K.1    Silver, J.2    Winchester, R.J.3
  • 2
    • 0002321272 scopus 로고
    • Immunogenetics and the rheumatic diseases
    • Edited by WN Kelley, ED Harris Jr, S Ruddy, CB Sledge. Philadelphia, WB Saunders
    • Nepom BS, Nepom GT: Immunogenetics and the rheumatic diseases. In, Textbook of Rheumatology. Edited by WN Kelley, ED Harris Jr, S Ruddy, CB Sledge. Philadelphia, WB Saunders, 1993
    • (1993) Textbook of Rheumatology
    • Nepom, B.S.1    Nepom, G.T.2
  • 4
    • 0029019662 scopus 로고
    • The importance of DR4Dw4 beta chain residues 70, 71, and 86 in peptide binding and T cell recognition
    • Signorelli KL, Watts LM, Lambert LE: The importance of DR4Dw4 beta chain residues 70, 71, and 86 in peptide binding and T cell recognition. Cell Immunol 162:217-224, 1995
    • (1995) Cell Immunol , vol.162 , pp. 217-224
    • Signorelli, K.L.1    Watts, L.M.2    Lambert, L.E.3
  • 7
    • 0029945544 scopus 로고    scopus 로고
    • A structural model for TCR recognition of the HLA class II shared epitope sequence implicated in susceptibility to rheumatoid arthritis
    • Penzotti JE, Doherty D, Lybrand TP, Nepom GT: A structural model for TCR recognition of the HLA class II shared epitope sequence implicated in susceptibility to rheumatoid arthritis. J Autoimmun 9:287-293, 1996
    • (1996) J Autoimmun , vol.9 , pp. 287-293
    • Penzotti, J.E.1    Doherty, D.2    Lybrand, T.P.3    Nepom, G.T.4
  • 8
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman DA, Case DA, Caldwell JW, Ross WS, Cheatham TE III, DeBolt S, Ferguson D, Seibel G, Kollman P: AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput Phys Commun 91:1-41, 1995
    • (1995) Comput Phys Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham III, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 9
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner SJ, Kollman PA, Nguyen DT, Case DA: An all atom force field for simulations of proteins and nucleic acids. J Comp Chem 7:230-252, 1986
    • (1986) J Comp Chem , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 10
    • 0023155210 scopus 로고
    • Tertiary templates for proteins: Use of packing in the enumeration of allowed sequences for different structural classes
    • Ponder JW, Richards FM: Tertiary templates for proteins: use of packing in the enumeration of allowed sequences for different structural classes. J Mol Biol 193:775-791, 1987
    • (1987) J Mol Biol , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 11
    • 0025269891 scopus 로고
    • Novel method for the rapid evaluation of packing in protein structures
    • Gregoret LM, Cohen FE: Novel method for the rapid evaluation of packing in protein structures. J Mol Biol 211:959-974, 1990
    • (1990) J Mol Biol , vol.211 , pp. 959-974
    • Gregoret, L.M.1    Cohen, F.E.2
  • 14
    • 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 267:1984-1987, 1995
    • (1995) Science , vol.267 , pp. 1984-1987
    • Bentley, G.A.1    Boulot, G.2    Karjalainen, K.3    Mariuzza, R.A.4
  • 15
    • 0027049523 scopus 로고
    • Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2
    • Tormo J, Stadler E, Skern T, Auer H, Kanzler O, Betzel C, Blaas D, Fita I: Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2. Protein Sci 1:1154-1161, 1992
    • (1992) Protein Sci , vol.1 , pp. 1154-1161
    • Tormo, J.1    Stadler, E.2    Skern, T.3    Auer, H.4    Kanzler, O.5    Betzel, C.6    Blaas, D.7    Fita, I.8
  • 16
    • 0019119230 scopus 로고
    • Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.0 Å resolution
    • Marquart M, Deisenhofer J, Huber R, Palm W: Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.0 Å resolution. J Mol Biol 141:369-391, 1980
    • (1980) J Mol Biol , vol.141 , pp. 369-391
    • Marquart, M.1    Deisenhofer, J.2    Huber, R.3    Palm, W.4
  • 17
    • 0025398721 scopus 로고
    • WHATIF: A molecular modeling and drug design program
    • Vriend G: WHATIF: a molecular modeling and drug design program. J Mol Graph 8:52-56, 1990
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 20
    • 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 7:3745-3755, 1988
    • (1988) EMBO J , vol.7 , pp. 3745-3755
    • Chothia, C.1    Boswell, D.R.2    Lesk, A.M.3
  • 22
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly ML: Solvent-accessible surfaces of proteins and nucleic acids. Science 221:709-713, 1983
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 23
    • 0023720148 scopus 로고
    • T-cell antigen receptor genes and T-cell recognition
    • Davis MM, Bjorkman PJ: T-cell antigen receptor genes and T-cell recognition. Nature 334:395-402, 1988
    • (1988) Nature , vol.334 , pp. 395-402
    • Davis, M.M.1    Bjorkman, P.J.2
  • 25
    • 0029082524 scopus 로고
    • Molecular modeling of a T-cell receptor bound to a major histocompatibility complex molecule: Implications for T-cell recognition
    • Almagro JC, Vargas-Madrazo E, Lara-Ochoa F, Horjales E: Molecular modeling of a T-cell receptor bound to a major histocompatibility complex molecule: implications for T-cell recognition. Protein Sci 4:1708-1717, 1995
    • (1995) Protein Sci , vol.4 , pp. 1708-1717
    • Almagro, J.C.1    Vargas-Madrazo, E.2    Lara-Ochoa, F.3    Horjales, E.4
  • 26
    • 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 384:134-141, 1996
    • (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
  • 27
    • 0016804680 scopus 로고
    • The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution
    • Epp O, Lattman EE, Schiffer M, Huber R, Palm W: The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution. Biochemistry 14:4943-4952, 1975
    • (1975) Biochemistry , vol.14 , pp. 4943-4952
    • Epp, O.1    Lattman, E.E.2    Schiffer, M.3    Huber, R.4    Palm, W.5
  • 28
    • 0027325038 scopus 로고
    • Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen
    • Rini JM, Stanfield RL, Stura EA, Salinas PA, Profy AT, Wilson IA: Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen. Proc Natl Acad Sci U S A 90:6325-6329, 1993
    • (1993) Proc Natl Acad Sci U S a , vol.90 , pp. 6325-6329
    • Rini, J.M.1    Stanfield, R.L.2    Stura, E.A.3    Salinas, P.A.4    Profy, A.T.5    Wilson, I.A.6
  • 30
    • 0024329804 scopus 로고
    • Three-dimensional structure of a fluorescein-Fab complex crystallized in 2-methyl-2,4-pentanediol
    • Herron JN, He XM, Mason ML, Voss EW Jr, Edmundson AB: Three-dimensional structure of a fluorescein-Fab complex crystallized in 2-methyl-2,4-pentanediol. Proteins 5:271-280, 1989
    • (1989) Proteins , vol.5 , pp. 271-280
    • Herron, J.N.1    He, X.M.2    Mason, M.L.3    Voss Jr., E.W.4    Edmundson, A.B.5
  • 35
    • 0027532161 scopus 로고
    • Predicting the size of the T-cell receptor and antibody combining region from consideration of efficient self-nonself discrimination
    • Percus JK, Percus OE, Perelson AS: Predicting the size of the T-cell receptor and antibody combining region from consideration of efficient self-nonself discrimination. Proc Natl Acad Sci U S A 90:1691-1695, 1993
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 1691-1695
    • Percus, J.K.1    Percus, O.E.2    Perelson, A.S.3
  • 36
    • 0025597053 scopus 로고
    • Delineation of antigen contact residues on an MHC class II molecule
    • Peccoud J, Dellabona P, Allen P, Benoist C, Mathis D: Delineation of antigen contact residues on an MHC class II molecule. EMBO J 9:4215-4223, 1990
    • (1990) EMBO J , vol.9 , pp. 4215-4223
    • Peccoud, J.1    Dellabona, P.2    Allen, P.3    Benoist, C.4    Mathis, D.5
  • 38
    • 0025018298 scopus 로고
    • Superantigens interact with MHC class II molecules outside of the antigen groove
    • Dellabona P, Peccoud J, Kappler J, Marrack P, Benoist C, Mathis D: Superantigens interact with MHC class II molecules outside of the antigen groove. Cell 62:1115-1121, 1990
    • (1990) Cell , vol.62 , pp. 1115-1121
    • Dellabona, P.1    Peccoud, J.2    Kappler, J.3    Marrack, P.4    Benoist, C.5    Mathis, D.6
  • 39
  • 41
    • 0029939649 scopus 로고    scopus 로고
    • Oligoclonal T cell proliferation in patients with rheumatoid arthritis and their unaffected siblings
    • Waase I, Kayser C, Carlson PJ, Goronzy JJ, Weyand CM: Oligoclonal T cell proliferation in patients with rheumatoid arthritis and their unaffected siblings. Arthritis Rheum 39:904-913, 1996
    • (1996) Arthritis Rheum , vol.39 , pp. 904-913
    • Waase, I.1    Kayser, C.2    Carlson, P.J.3    Goronzy, J.J.4    Weyand, C.M.5
  • 42
    • 0029079836 scopus 로고
    • A review of T-cell receptors in multiple sclerosis: Clonal expansion and persistence of human T-cells specific for an immunodominant myelin basic protein peptide
    • Wucherpfennig KW, Hafler DA: A review of T-cell receptors in multiple sclerosis: clonal expansion and persistence of human T-cells specific for an immunodominant myelin basic protein peptide. Ann N Y Acad Sci 756:241-258, 1995
    • (1995) Ann N Y Acad Sci , vol.756 , pp. 241-258
    • Wucherpfennig, K.W.1    Hafler, D.A.2
  • 43
    • 0028007176 scopus 로고
    • CDR3 sequence motifs shared by oligoclonal rheumatoid arthritis synovial T cells: Evidence for an antigen-driven response
    • Li Y, Sun GR, Tumang JR, Crow MK, Friedman SM: CDR3 sequence motifs shared by oligoclonal rheumatoid arthritis synovial T cells: evidence for an antigen-driven response. J Clin Invest 94:2525-2531, 1994
    • (1994) J Clin Invest , vol.94 , pp. 2525-2531
    • Li, Y.1    Sun, G.R.2    Tumang, J.R.3    Crow, M.K.4    Friedman, S.M.5
  • 44
    • 0029074729 scopus 로고
    • Structure of human T-cell receptors specific for an immunodominant myelin basic protein peptide: Positioning of T-cell receptors on HLA-DR2/peptide complexes
    • Wucherpfennig KW, Hafler DA, Strominger JL: Structure of human T-cell receptors specific for an immunodominant myelin basic protein peptide: positioning of T-cell receptors on HLA-DR2/peptide complexes. Proc Natl Acad Sci U S A 92:8896-8900, 1995
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8896-8900
    • Wucherpfennig, K.W.1    Hafler, D.A.2    Strominger, J.L.3
  • 45
  • 46
    • 0026502380 scopus 로고
    • Mapping T-cell receptor-peptide contacts by variant peptide immunization of single-chain transgenics
    • Jorgensen JL, Esser U, Fazekas de St. Groth B, Reay PA, Davis MM: Mapping T-cell receptor-peptide contacts by variant peptide immunization of single-chain transgenics. Nature 355:224-230, 1992
    • (1992) Nature , vol.355 , pp. 224-230
    • Jorgensen, J.L.1    Esser, U.2    Fazekas De St. Groth, B.3    Reay, P.A.4    Davis, M.M.5
  • 47
    • 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: The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378:457-462, 1995
    • (1995) Nature , vol.378 , pp. 457-462
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 48
    • 0030069683 scopus 로고    scopus 로고
    • Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides
    • Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, Strominger JL, Wiley DC: Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc Natl Acad Sci U S A 93:734-738, 1996
    • (1996) Proc Natl Acad Sci U S a , vol.93 , pp. 734-738
    • Jardetzky, T.S.1    Brown, J.H.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 49
    • 0026552084 scopus 로고
    • Functional analysis of the antigen binding site on the T cell receptor alpha chain
    • Nalefski EA, Kasibhatla S, Rao A: Functional analysis of the antigen binding site on the T cell receptor alpha chain. J Exp Med 175:1553-1563, 1992
    • (1992) J Exp Med , vol.175 , pp. 1553-1563
    • Nalefski, E.A.1    Kasibhatla, S.2    Rao, A.3
  • 51
    • 0029896115 scopus 로고    scopus 로고
    • Modulation of promiscuous T cell receptor recognition by mutagenesis of CDR2 residues
    • Brawley JV, Concannon P: Modulation of promiscuous T cell receptor recognition by mutagenesis of CDR2 residues. J Exp Med 183:2043-2051, 1996
    • (1996) J Exp Med , vol.183 , pp. 2043-2051
    • Brawley, J.V.1    Concannon, P.2
  • 52
    • 0028261582 scopus 로고
    • Use of global amino acid replacements to define the requirements for MHC binding and T cell recognition of moth cytochrome c (93-103)
    • Reay PA, Kantor RM, Davis MM: Use of global amino acid replacements to define the requirements for MHC binding and T cell recognition of moth cytochrome c (93-103). J Immunol 152:3946-3957, 1994
    • (1994) J Immunol , vol.152 , pp. 3946-3957
    • Reay, P.A.1    Kantor, R.M.2    Davis, M.M.3
  • 53
    • 0025283333 scopus 로고
    • The presumptive CDR3 regions of both T cell receptor α and β chains determine T cell specificity for myoglobin peptides
    • Danska JS, Livingstone AM, Paragas V, Ishihara T, Fathman CG: The presumptive CDR3 regions of both T cell receptor α and β chains determine T cell specificity for myoglobin peptides. J Exp Med 172:27-33, 1990
    • (1990) J Exp Med , vol.172 , pp. 27-33
    • Danska, J.S.1    Livingstone, A.M.2    Paragas, V.3    Ishihara, T.4    Fathman, C.G.5
  • 58
    • 0025840491 scopus 로고
    • Limited T-cell receptor beta-chain heterogeneity among interleukin 2 receptor-positive synovial T cells suggests a role for superantigen in rheumatoid arthritis
    • Howell MD, Diveley JP, Lundeen KA, Esty A, Winters ST, Carlo DJ, Brostoff SW: Limited T-cell receptor beta-chain heterogeneity among interleukin 2 receptor-positive synovial T cells suggests a role for superantigen in rheumatoid arthritis. Proc Natl Acad Sci U S A 88:10921-10925, 1991
    • (1991) Proc Natl Acad Sci U S a , vol.88 , pp. 10921-10925
    • Howell, M.D.1    Diveley, J.P.2    Lundeen, K.A.3    Esty, A.4    Winters, S.T.5    Carlo, D.J.6    Brostoff, S.W.7
  • 60
    • 0029092766 scopus 로고
    • Deficient antigen-presenting cell function in multiple genetic complementation groups of type II bare lymphocyte syndrome
    • Kovats S, Nepom GT, Coleman M, Nepom B, Kwok WW, Blum JS: Deficient antigen-presenting cell function in multiple genetic complementation groups of type II bare lymphocyte syndrome. J Clin Invest 96:217-223, 1995
    • (1995) J Clin Invest , vol.96 , pp. 217-223
    • Kovats, S.1    Nepom, G.T.2    Coleman, M.3    Nepom, B.4    Kwok, W.W.5    Blum, J.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.