메뉴 건너뛰기




Volumn 16, Issue 14, 1997, Pages 4205-4216

The three-dimensional structure of a T-cell antigen receptor VαVβ heterodimer reveals a novel arrangement of the Vβ domain

Author keywords

Antigen binding site; Complementarity determining region; Crystal structure; Fv fragment; T cell receptor

Indexed keywords

DIMER; IMMUNOGLOBULIN F(AB) FRAGMENT; T LYMPHOCYTE RECEPTOR;

EID: 0030855425     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.14.4205     Document Type: Article
Times cited : (87)

References (60)
  • 1
    • 0020371569 scopus 로고
    • Interactions between MHC-encoded products and cloned T-cells. I. Fine specificity of induction of proliferation and lysis
    • Albert, F., Buferne, M., Boyer, C. and Schmitt-Verhulst, A.-M. (1982) Interactions between MHC-encoded products and cloned T-cells. I. Fine specificity of induction of proliferation and lysis. Immunogenetics, 16, 533-549.
    • (1982) Immunogenetics , vol.16 , pp. 533-549
    • Albert, F.1    Buferne, M.2    Boyer, C.3    Schmitt-Verhulst, A.-M.4
  • 3
    • 0025059666 scopus 로고
    • Three-dimensional structure of an idiotope-anti-idiotope complex
    • Bentley, G.A., Boulot, G., Riottot, M.M. and Poljak, R.J. (1990) Three-dimensional structure of an idiotope-anti-idiotope complex. Nature, 348, 254-257.
    • (1990) Nature , vol.348 , pp. 254-257
    • Bentley, G.A.1    Boulot, G.2    Riottot, M.M.3    Poljak, R.J.4
  • 4
    • 0028956603 scopus 로고
    • Crystal structure of the β chain of a T cell antigen receptor
    • Bentley, G.A., Boulot, G., Karjalainen, K. and Mariuzza, R.A. (1995) Crystal structure of the β chain of a T cell antigen receptor. Science, 267, 1984-1987.
    • (1995) Science , vol.267 , pp. 1984-1987
    • Bentley, G.A.1    Boulot, G.2    Karjalainen, K.3    Mariuzza, R.A.4
  • 6
    • 0028014642 scopus 로고
    • Bound water molecules and conformational stabilization help mediate an antigen-antibody association
    • Bhat, T.N. et al. (1994) Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Proc. Natl Acad. Sci. USA, 91, 1089-1093.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1089-1093
    • Bhat, T.N.1
  • 7
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork, P., Holm, L. and Sander, C. (1994) The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol., 242, 309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 8
    • 0027971497 scopus 로고
    • Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1
    • Braden, B.C., Souchon, H., Eisele, J.L., Bentley, G.A., Bhat, T.N., Navaza, J. and Poljak, R.J. (1994) Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1. J. Mol. Biol., 243, 767-781.
    • (1994) J. Mol. Biol. , vol.243 , pp. 767-781
    • Braden, B.C.1    Souchon, H.2    Eisele, J.L.3    Bentley, G.A.4    Bhat, T.N.5    Navaza, J.6    Poljak, R.J.7
  • 13
    • 0022339938 scopus 로고
    • Domain association in immunoglobulin molecules. The packing of variable domains
    • Chothia, C., Novotny, J., Bruccoleri, R. and Karplus, M. (1985) Domain association in immunoglobulin molecules. The packing of variable domains. J. Mol. Biol. 186, 651-663.
    • (1985) J. Mol. Biol. , vol.186 , pp. 651-663
    • Chothia, C.1    Novotny, J.2    Bruccoleri, R.3    Karplus, M.4
  • 14
    • 2642648459 scopus 로고
    • The outline structure of the T-cell αβ receptor
    • Chothia, C., Boswell, D.R. and Lesk, M.A. (1988) The outline structure of the T-cell αβ receptor. EMBO J., 7, 3745-3755.
    • (1988) EMBO J. , vol.7 , pp. 3745-3755
    • Chothia, C.1    Boswell, D.R.2    Lesk, M.A.3
  • 15
    • 0024844388 scopus 로고
    • Conformations of immunoglobulin hypervariable regions
    • Chothia, C. et al. (1989) Conformations of immunoglobulin hypervariable regions. Nature, 342, 877-883.
    • (1989) Nature , vol.342 , pp. 877-883
    • Chothia, C.1
  • 16
    • 0029558857 scopus 로고
    • Comparison of human and mouse T-cell receptor variable gene segments families
    • Clark, S.P., Arden, B., Kabelitz, D. and Mak, T.W. (1995) Comparison of human and mouse T-cell receptor variable gene segments families. Immunogenetics, 42, 531-540.
    • (1995) Immunogenetics , vol.42 , pp. 531-540
    • Clark, S.P.1    Arden, B.2    Kabelitz, D.3    Mak, T.W.4
  • 18
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies, D.R. and Cohen, G.H. (1996) Interactions of protein antigens with antibodies. Proc. Natl Acad. Sci. USA, 93, 7-12.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 19
    • 0023720148 scopus 로고
    • T-cell antigen receptor genes and T-cell recognition
    • Davis, M.M. and Bjorkman, P.J. (1988) T-cell antigen receptor genes and T-cell recognition. Nature, 334, 395-401.
    • (1988) Nature , vol.334 , pp. 395-401
    • Davis, M.M.1    Bjorkman, P.J.2
  • 20
    • 0029417003 scopus 로고
    • Crystal structure of the Vα domain of a T cell antigen receptor
    • Fields, B.A. et al. (1995) Crystal structure of the Vα domain of a T cell antigen receptor. Science, 270, 1821-1824.
    • (1995) Science , vol.270 , pp. 1821-1824
    • Fields, B.A.1
  • 23
    • 0028987213 scopus 로고
    • b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove
    • b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl Acad. Sci. USA, 92, 2479-2483.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2479-2483
    • Fremont, D.H.1    Stura, E.A.2    Matsumura, M.3    Peterson, P.A.4    Wilson, I.A.5
  • 25
    • 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. (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.6
  • 28
    • 0029552310 scopus 로고
    • Increased peptide promiscuity provides a rationale for the lack of N regions in the neonatal T cell repertoire
    • Gavin, M.A. and Bevan, M.J. (1995) Increased peptide promiscuity provides a rationale for the lack of N regions in the neonatal T cell repertoire. Immunity, 3, 793-800.
    • (1995) Immunity , vol.3 , pp. 793-800
    • Gavin, M.A.1    Bevan, M.J.2
  • 31
    • 0029819959 scopus 로고    scopus 로고
    • Characterization of T cell receptor single-chain Fv fragments secreted by myeloma cells
    • Grégoire, C., Malissen, B. and Mazza, G. (1996) Characterization of T cell receptor single-chain Fv fragments secreted by myeloma cells. Eur. J. Immunol., 26, 2410-2416.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2410-2416
    • Grégoire, C.1    Malissen, B.2    Mazza, G.3
  • 32
    • 0026554421 scopus 로고
    • A viral peptide can mimic an endogeneous peptide for allorecognition of a major histocompatibility complex class 1 product
    • Guimezanes, A., Schumacher, T.N.M., Ploegh, H.L. and Schmitt-Verhulst, A.-M. (1992) A viral peptide can mimic an endogeneous peptide for allorecognition of a major histocompatibility complex class 1 product. Eur. J. Immunol., 22, 1651-1654.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1651-1654
    • Guimezanes, A.1    Schumacher, T.N.M.2    Ploegh, H.L.3    Schmitt-Verhulst, A.-M.4
  • 33
    • 0028463920 scopus 로고
    • Calibration and correction of spatial distortions in 2D detector systems
    • Hammersley, A.P., Svensson, S.O. and Thompson, A. (1994) Calibration and correction of spatial distortions in 2D detector systems. Nucl. Instrum. Methods A, 346, 312-321.
    • (1994) Nucl. Instrum. Methods A , vol.346 , pp. 312-321
    • Hammersley, A.P.1    Svensson, S.O.2    Thompson, A.3
  • 34
    • 0021934381 scopus 로고
    • Lysis of hybridoma cells bearing anti-clonotypic surface immunoglobulin by clonotype-expressing alloreactive cytotoxic T cells
    • Hua, C. Buferne, M. and Schmitt-Verhulst, A.-M. (1985) Lysis of hybridoma cells bearing anti-clonotypic surface immunoglobulin by clonotype-expressing alloreactive cytotoxic T cells. Eur. J. Immunol., 15, 1029-1032.
    • (1985) Eur. J. Immunol. , vol.15 , pp. 1029-1032
    • Hua, C.1    Buferne, M.2    Schmitt-Verhulst, A.-M.3
  • 35
    • 0025286125 scopus 로고
    • A novel type of aberrant T cell receptor α-chain gene rearrangement. Implications for allelic exclusion and the V-J recombination process
    • Hue, I., Trucy, J., McCoy, C., Couez, D., Malissen, B. and Malissen, M. (1990) A novel type of aberrant T cell receptor α-chain gene rearrangement. Implications for allelic exclusion and the V-J recombination process. J. Immunol., 144, 4410-4419.
    • (1990) J. Immunol. , vol.144 , pp. 4410-4419
    • Hue, I.1    Trucy, J.2    McCoy, C.3    Couez, D.4    Malissen, B.5    Malissen, M.6
  • 36
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 37
    • 0025612174 scopus 로고
    • Resolution of hypervariable regions in T-cell receptor β chains by a modified Wu-Kabat index of amino acid diversity
    • Jores, R., Alzari, P.M. and Meo, T. (1990) Resolution of hypervariable regions in T-cell receptor β chains by a modified Wu-Kabat index of amino acid diversity. Proc. Natl Acad. Sci. USA, 87, 9138-9142.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9138-9142
    • Jores, R.1    Alzari, P.M.2    Meo, T.3
  • 39
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction data from a position sensitive detector
    • Kabsch, W. (1988) Evaluation of single crystal X-ray diffraction data from a position sensitive detector. J. Appl. Crystallogr., 21, 916-924.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 40
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr., 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 41
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 43
    • 0002414103 scopus 로고
    • Molecular data processing
    • Moras, D., Podjarny, A.D. and Thierry, J.C. (eds). Oxford University Press
    • Leslie, A.G.W. (1991) Molecular data processing. In Moras, D., Podjarny, A.D. and Thierry, J.C. (eds). Crystallographic Computing. Oxford University Press, pp. 50-61.
    • (1991) Crystallographic Computing , pp. 50-61
    • Leslie, A.G.W.1
  • 44
    • 0028797801 scopus 로고    scopus 로고
    • CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes
    • Luescher, I.F., Vivier, E., Layer, A., Mahiou, J., Godeau, F., Malissen, B. and Romero, P. (1996) CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes. Nature, 373, 353-356.
    • (1996) Nature , vol.373 , pp. 353-356
    • Luescher, I.F.1    Vivier, E.2    Layer, A.3    Mahiou, J.4    Godeau, F.5    Malissen, B.6    Romero, P.7
  • 45
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden, D.R., Garboczi, D.J. and Wiley, D.C. (1993) The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell, 75, 693-708.
    • (1993) Cell , vol.75 , pp. 693-708
    • Madden, D.R.1    Garboczi, D.J.2    Wiley, D.C.3
  • 46
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968) Solvent content of protein crystals. J. Mol. Biol., 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 47
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr., A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 48
    • 0019312916 scopus 로고
    • Organization and complete sequence of identical embryonic and plasmacytoma kappa V-region genes
    • Nishioka, Y. and Leder, P. (1980) Organization and complete sequence of identical embryonic and plasmacytoma kappa V-region genes. J. Biol. Chem., 255, 3691-3694.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3691-3694
    • Nishioka, Y.1    Leder, P.2
  • 49
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan, E.A. (1994) Anatomy of the antibody molecule. Mol. Immunol., 31, 169-217.
    • (1994) Mol. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 50
    • 0027251463 scopus 로고
    • The sizes of the CDR3 hypervariable regions of the murine T-cell receptor β chains vary as a function of the recombined germ-line segments
    • Pannetier, C., Cochet, M., Darche, S., Casrouge, A., Zöller, M. and Kourilsky, P. (1993) The sizes of the CDR3 hypervariable regions of the murine T-cell receptor β chains vary as a function of the recombined germ-line segments. Proc. Natl Acad. Sci. USA, 90, 4319-4323.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4319-4323
    • Pannetier, C.1    Cochet, M.2    Darche, S.3    Casrouge, A.4    Zöller, M.5    Kourilsky, P.6
  • 51
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R. (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr., A42, 140-149.
    • (1986) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Read, R.1
  • 52
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603: An X-ray diffraction study at 2.7 Å
    • Satow, Y., Cohen, G.H., Padlan, E.A. and Davies, D. (1986) Phosphocholine binding immunoglobulin Fab McPC603: an X-ray diffraction study at 2.7 Å. J. Mol. Biol., 190, 593-604.
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.4
  • 53
    • 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.J. (1996) Control of MHC restriction by TCR Vα CDR1 and CDR2. Science, 273, 963-966.
    • (1996) Science , vol.273 , pp. 963-966
    • Sim, B.-C.1    Zerva, L.2    Greene, M.I.3    Gascoigne, N.R.J.4
  • 55
    • 0029840391 scopus 로고    scopus 로고
    • A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity
    • Tallquist, M., Yun, T.J. and Pease, L.R. (1996) A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity. J. Exp. Med., 184, 1017-1026.
    • (1996) J. Exp. Med. , vol.184 , pp. 1017-1026
    • Tallquist, M.1    Yun, T.J.2    Pease, L.R.3
  • 56
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells, J.A. (1996) Binding in the growth hormone receptor complex. Proc. Natl Acad. Sci. USA, 93, 1-6.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 58
    • 0016434857 scopus 로고
    • Crystallisation and crystal data of monellin
    • Wlodawer, A. and Hodgson, K.O. (1975) Crystallisation and crystal data of monellin. Proc. Natl Acad. Sci. USA, 72, 398-399.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 398-399
    • Wlodawer, A.1    Hodgson, K.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.