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Volumn 9780387729688, Issue , 2008, Pages 19-49

IMGT standardization for molecular characterization of the T-cell receptor/peptide/MHC complexes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; CHAINS; IMMUNOLOGY; ONTOLOGY; PEPTIDES; STANDARDIZATION;

EID: 46049113012     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-72968-8_2     Document Type: Chapter
Times cited : (21)

References (56)
  • 1
    • 0029096589 scopus 로고
    • Prediction of binding to MHC class I molecules
    • Adams, H. P., and Koziol, J. A. (1995) Prediction of binding to MHC class I molecules. J. Immunol. Methods 185:181-190.
    • (1995) J. Immunol. Methods , vol.185 , pp. 181-190
    • Adams, H.P.1    Koziol, J.A.2
  • 2
    • 0036311017 scopus 로고    scopus 로고
    • Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: A new approach for vaccine design
    • Apostolopoulos, V., Yu, M., Corper, A. L., Teyton, L., Pieters, G. A., McKenzie, I. F. C., and Wilson, I. A. (2002) Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: A new approach for vaccine design. J. Mol. Biol. 318:1293-1305.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1293-1305
    • Apostolopoulos, V.1    Yu, M.2    Corper, A.L.3    Teyton, L.4    Pieters, G.A.5    McKenzie, I.F.C.6    Wilson, I.A.7
  • 5
    • 0036211926 scopus 로고    scopus 로고
    • JenPep: A database of quantitative functional peptide data for immunology
    • Blythe, M. J., Doytchinova, I. A., and Flower, D. R. (2002) JenPep: A database of quantitative functional peptide data for immunology. Bioinformatics 18:434-439.
    • (2002) Bioinformatics , vol.18 , pp. 434-439
    • Blythe, M.J.1    Doytchinova, I.A.2    Flower, D.R.3
  • 6
    • 0031811850 scopus 로고    scopus 로고
    • MHCPEP, a database of MHC-binding peptides: Update 1997
    • Brusic, V., Rudy, G., and Harrison, L. C. (1998) MHCPEP, a database of MHC-binding peptides: Update 1997. Nucleic Acids Res. 26:368-371.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 368-371
    • Brusic, V.1    Rudy, G.2    Harrison, L.C.3
  • 7
    • 0142219443 scopus 로고    scopus 로고
    • A correlation between TCR Vα docking on MHC and CD8 dependence: Implications for T cell selection
    • Buslepp, J., Wang, H., Biddison, W. E., Appella, E., and Collins, E. J. (2003) A correlation between TCR Vα 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
  • 8
    • 0037047353 scopus 로고    scopus 로고
    • A new trigger for T cells
    • Davis, M. M. (2002) A new trigger for T cells. Cell 110:285-287.
    • (2002) Cell , vol.110 , pp. 285-287
    • Davis, M.M.1
  • 10
    • 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, Y. H., Smith, K. J., Garboczi, D. N., Utz, U., Biddison, W. E., and Wiley, D. C. (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    Wiley, D.C.6
  • 11
    • 0033165928 scopus 로고    scopus 로고
    • Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
    • Ding, Y. H., Baker, B. M., Garboczi, D. N., Biddison, W. E., and Wiley, D. C. (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
  • 12
    • 0025855156 scopus 로고
    • Allelespecific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk, K., Rotzschke, O., Stevanovic, S., Jung, G., and Rammensee, H. G. (1991) Allelespecific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351:290-296.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.G.5
  • 13
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi, D. N., Ghosh, P., Utz, U., Fan, Q. R., Biddison, W. E., and Wiley, D. C. (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    Wiley, D.C.6
  • 15
    • 0033493024 scopus 로고    scopus 로고
    • Ontology for immunogenetics: The IMGT-ONTOLOGY
    • Giudicelli, V., and Lefranc, M.-P. (1999) Ontology for immunogenetics: The IMGT-ONTOLOGY. Bioinformatics 15:1047-1054.
    • (1999) Bioinformatics , vol.15 , pp. 1047-1054
    • Giudicelli, V.1    Lefranc, M.-P.2
  • 16
    • 3242876679 scopus 로고    scopus 로고
    • IMGT/V-QUEST, an integrated software program for immunoglobulin and T cell receptor V-J and V-D-J rearrangement analysis
    • Giudicelli, V., Chaume, D., and Lefranc, M.-P. (2004) IMGT/V-QUEST, an integrated software program for immunoglobulin and T cell receptor V-J and V-D-J rearrangement analysis. Nucleic Acids Res. 32:435-440.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 435-440
    • Giudicelli, V.1    Chaume, D.2    Lefranc, M.-P.3
  • 17
    • 13444273444 scopus 로고    scopus 로고
    • IMGT/GENE-DB: A comprehensive database for human and mouse immunoglobulin and T cell receptor genes
    • Giudicelli, V., Chaume, D., and Lefranc, M.-P. (2005) IMGT/GENE-DB: A comprehensive database for human and mouse immunoglobulin and T cell receptor genes. Nucleic Acids Res. 33:256-261.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 256-261
    • Giudicelli, V.1    Chaume, D.2    Lefranc, M.-P.3
  • 18
    • 33644874839 scopus 로고    scopus 로고
    • IMGT/LIGM-DB, the IMGT® comprehensive database of immunoglobulin and T cell receptor nucleotide sequences
    • Giudicelli, V., Ginestoux, C., Folch, G., Jabado-Michaloud, J., Chaume, D., and Lefranc, M.-P. (2006) IMGT/LIGM-DB, the IMGT® comprehensive database of immunoglobulin and T cell receptor nucleotide sequences. Nucleic Acids Res. 34:D781-D784.
    • (2006) Nucleic Acids Res. , vol.34 , pp. D781-D784
    • Giudicelli, V.1    Ginestoux, C.2    Folch, G.3    Jabado-Michaloud, J.4    Chaume, D.5    Lefranc, M.-P.6
  • 19
    • 0031576987 scopus 로고    scopus 로고
    • Two complementary methods for predicting peptides binding major histocompatibility complex molecules
    • Gulukota, K., Sidney, J., Sette, A., and De Lisi, C. (1997) Two complementary methods for predicting peptides binding major histocompatibility complex molecules. J. Mol. Biol. 267:1258-1267.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1258-1267
    • Gulukota, K.1    Sidney, J.2    Sette, A.3    De Lisi, C.4
  • 20
    • 0034329441 scopus 로고    scopus 로고
    • Structure of a covalently stabilized complex of a human αβ T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
    • Hennecke, J., Carfi, A., and Wiley, D. C. (2000) Structure of a covalently stabilized complex of a human αβ 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
  • 21
    • 0037018102 scopus 로고    scopus 로고
    • ∗0401): Insight into TCR cross-restriction and alloreactivity
    • ∗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
  • 22
    • 0037167816 scopus 로고    scopus 로고
    • Direct observation of ligand recognition by T cells
    • Irvine, D. J., Purbhoo, M. A., Krosgaard, M., and Davis, M. M. (2002) Direct observation of ligand recognition by T cells. Nature 419:845-849.
    • (2002) Nature , vol.419 , pp. 845-849
    • Irvine, D.J.1    Purbhoo, M.A.2    Krosgaard, M.3    Davis, M.M.4
  • 23
    • 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., and Lefranc, M.-P. (2004) IMGT/3Dstructure-DB and IMGT/StructuralQuery, a database and a tool for immunoglobulin, T cell receptor and MHC structural data. Nucleic Acids Res. 32:208-210.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 208-210
    • Kaas, Q.1    Ruiz, M.2    Lefranc, M.-P.3
  • 24
    • 32544458887 scopus 로고    scopus 로고
    • T cell receptor/peptide/MHC molecular characterization and standardized pMHC contact sites in IMGT/3Dstructure-DB
    • Kaas, Q., and Lefranc, M.-P. (2005) T cell receptor/peptide/MHC molecular characterization and standardized pMHC contact sites in IMGT/3Dstructure-DB. In Silico Biol. 5:505-528.
    • (2005) Silico Biol. , vol.5 , pp. 505-528
    • Kaas, Q.1    Lefranc, M.-P.2
  • 26
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M. C., and Colman, P. M. (1993) Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234:946-950.
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 28
    • 3242884935 scopus 로고    scopus 로고
    • IMGT, the international ImMunoGeneTics information system®
    • B. K. C. Lo Ed., 2nd edition. Methods in Molecular Biology. Humana Press, Totowa, NJ
    • Lefranc, M.-P. (2003a) IMGT, the international ImMunoGeneTics information system® (http://imgt.cines.fr). In: B. K. C. Lo (Ed.), Antibody Engineering: Methods and Protocols, 2nd edition. Methods in Molecular Biology. Humana Press, Totowa, NJ, 248, pp. 27-49.
    • (2003) Antibody Engineering: Methods and Protocols , vol.248 , pp. 27-49
    • Lefranc, M.-P.1
  • 30
    • 0345276458 scopus 로고    scopus 로고
    • IMGT-ONTOLOGY and IMGT databases, tools and Web resources for immunogenetics and immunoinformatics
    • Lefranc, M.-P. (2004a) IMGT-ONTOLOGY and IMGT databases, tools and Web resources for immunogenetics and immunoinformatics. Mol. Immunol. 40:647-660.
    • (2004) Mol. Immunol. , vol.40 , pp. 647-660
    • Lefranc, M.-P.1
  • 33
    • 21444450056 scopus 로고    scopus 로고
    • IMGT unique numbering for MHC groove G-DOMAIN and MHC superfamily (MhcSF) G-LIKE-DOMAIN
    • Lefranc, M.-P., Duprat, E., Kaas, Q., Tranne, M., Thiriot, A., and Lefranc, G. (2005b) 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    Lefranc, G.6
  • 36
    • 0020429363 scopus 로고
    • Evolution of proteins formed by β-sheets. II. The core of the immunoglobulin domains
    • Lesk, A. M., and Chothia, C. (1982) Evolution of proteins formed by β-sheets. II. The core of the immunoglobulin domains. J. Mol. Biol. 160:325-342.
    • (1982) J. Mol. Biol. , vol.160 , pp. 325-342
    • Lesk, A.M.1    Chothia, C.2
  • 37
    • 0037029674 scopus 로고    scopus 로고
    • Structural comparison of allogeneic and syngeneic T cell receptorpeptide-major histocompatibility complex complexes: A buried alloreactive mutation subtly alters peptide presentation substantially increasing V (β) interactions
    • Luz, J. G., Huang, M., Garcia, K. C., Rudolph, M. G., Apostolopoulos, V., Teyton, L., and Wilson, I. A. (2002) Structural comparison of allogeneic and syngeneic T cell receptorpeptide-major histocompatibility complex complexes: A buried alloreactive mutation subtly alters peptide presentation substantially increasing V (β) interactions. J. Exp. Med. 195:1175-1186.
    • (2002) J. Exp. Med. , vol.195 , pp. 1175-1186
    • Luz, J.G.1    Huang, M.2    Garcia, K.C.3    Rudolph, M.G.4    Apostolopoulos, V.5    Teyton, L.6    Wilson, I.A.7
  • 38
    • 0031573713 scopus 로고    scopus 로고
    • Identification of shared tumor-associated antigen peptides between two spontaneous lung carcinomas
    • Mandelboim, O., Bar-Haim, E., Vadai, E., Fridkin, M., and Eisenbach, L. (1997) Identification of shared tumor-associated antigen peptides between two spontaneous lung carcinomas. J. Immunol. 159:6030-6036.
    • (1997) J. Immunol. , vol.159 , pp. 6030-6036
    • Mandelboim, O.1    Bar-Haim, E.2    Vadai, E.3    Fridkin, M.4    Eisenbach, L.5
  • 46
    • 0032033678 scopus 로고    scopus 로고
    • Crystal structures of two I-Adpeptide complexes reveal that high affinity can be achieved without large anchor residues
    • Scott, C. A., Peterson, P. A., Teyton, L., and Wilson, I. A. (1998) Crystal structures of two I-Adpeptide complexes reveal that high affinity can be achieved without large anchor residues. Immunity 8:319-329.
    • (1998) Immunity , vol.8 , pp. 319-329
    • Scott, C.A.1    Peterson, P.A.2    Teyton, L.3    Wilson, I.A.4
  • 47
    • 0029791413 scopus 로고    scopus 로고
    • Control of MHC restriction by TCR Vα CDR1 and CDR2
    • Sim, B. C., Zerva, L., Greene, M. I., and Gascoigne, N. R. (1996) Control of MHC restriction by TCR Vα CDR1 and CDR2. Science 273:963-964.
    • (1996) Science , vol.273 , pp. 963-964
    • Sim, B.C.1    Zerva, L.2    Greene, M.I.3    Gascoigne, N.R.4
  • 48
    • 0037606124 scopus 로고    scopus 로고
    • ProPred1: Prediction of promiscuous MHC class-I binding sites
    • Singh, H., and Raghava, G. P. (2003) ProPred1: Prediction of promiscuous MHC class-I binding sites. Bioinformatics 19:1009-1014.
    • (2003) Bioinformatics , vol.19 , pp. 1009-1014
    • Singh, H.1    Raghava, G.P.2
  • 50
    • 0342699417 scopus 로고    scopus 로고
    • TcR recognition of the MHC-peptide dimer: Structural properties of a ternary complex
    • Vasmatzis, G., Cornette, J., Sezerman, U., and De Lisi, C. (1996a) TcR recognition of the MHC-peptide dimer: Structural properties of a ternary complex. J. Mol. Biol. 261:72-89.
    • (1996) J. Mol. Biol. , vol.261 , pp. 72-89
    • Vasmatzis, G.1    Cornette, J.2    Sezerman, U.3    De Lisi, C.4
  • 51
    • 0030292235 scopus 로고    scopus 로고
    • Computational determination of side chain specificity for pockets in class I MHC molecules
    • Vasmatzis, G., Zhang, C., Cornette, J. L., and De Lisi, C. (1996b) Computational determination of side chain specificity for pockets in class I MHC molecules. Mol. Immunol. 33:1231-1239.
    • (1996) Mol. Immunol. , vol.33 , pp. 1231-1239
    • Vasmatzis, G.1    Zhang, C.2    Cornette, J.L.3    De Lisi, C.4
  • 54
    • 0036229026 scopus 로고    scopus 로고
    • Structural basis of T cell recognition of peptides bound to MHC molecules
    • Wang, J. H., and Reinherz, E. L. (2002) Structural basis of T cell recognition of peptides bound to MHC molecules. Mol. Immunol. 38:1039-1049.
    • (2002) Mol. Immunol. , vol.38 , pp. 1039-1049
    • Wang, J.H.1    Reinherz, E.L.2
  • 55
    • 9644277298 scopus 로고    scopus 로고
    • IMGT/JunctionAnalysis: The first tool for the analysis of the immunoglobulin and T cell receptor complex V-J and V-D-J junctions
    • Yousfi Monod, M., Giudicelli, V., Chaume, D., and Lefranc, M.-P. (2004) IMGT/JunctionAnalysis: The first tool for the analysis of the immunoglobulin and T cell receptor complex V-J and V-D-J junctions. Bioinformatics 20:I379-I385.
    • (2004) Bioinformatics , vol.20 , pp. I379-I385
    • Yousfi Monod, M.1    Giudicelli, V.2    Chaume, D.3    Lefranc, M.-P.4
  • 56
    • 0032483463 scopus 로고    scopus 로고
    • Structural principles that govern the peptidebinding motifs of class I MHC molecules
    • Zhang, C., Anderson, A., and De Lisi, C. (1998) Structural principles that govern the peptidebinding motifs of class I MHC molecules. J. Mol. Biol. 281:929-947.
    • (1998) J. Mol. Biol. , vol.281 , pp. 929-947
    • Zhang, C.1    Anderson, A.2    De Lisi, C.3


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