메뉴 건너뛰기




Volumn 1, Issue 4, 2000, Pages 291-297

Crystal structure of a T cell receptor bound to an allogeneic MHC molecule

Author keywords

[No Author keywords available]

Indexed keywords

ALLOANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR;

EID: 5944249467     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/79728     Document Type: Article
Times cited : (192)

References (38)
  • 1
    • 0033581935 scopus 로고    scopus 로고
    • Selecting and maintaining a diverse T-cell repertoire
    • Goldrath, A. W. & Bevan, M. J. Selecting and maintaining a diverse T-cell repertoire. Nature 402, 255-262 (1999).
    • (1999) Nature , vol.402 , pp. 255-262
    • Goldrath, A.W.1    Bevan, M.J.2
  • 2
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia, K. C. et al. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279, 1166-1172 (1998).
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1
  • 3
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi, D. N. et al. 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
  • 4
    • 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. et al. 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, 1-20 (1998).
    • (1998) Immunity , vol.8 , pp. 1-20
    • Ding, Y.H.1
  • 5
    • 0034678142 scopus 로고    scopus 로고
    • Role of the 2C T cell receptor residues in the binding of self- And allo-major histocompatibility complexes
    • Lee, P. U. Y., Churchill, H. R. O., Daniels, M., Jameson, S. & Kranz, D. Role of the 2C T cell receptor residues in the binding of self- and allo-major histocompatibility complexes. J. Exp. Med. 191, 1355-1364 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1355-1364
    • Lee, P.U.Y.1    Churchill, H.R.O.2    Daniels, M.3    Jameson, S.4    Kranz, D.5
  • 6
    • 0028069388 scopus 로고
    • CDR3 length in antigen-specific immune receptors
    • Rock E. P., Sibbald, P. R., Davis, M. M. & Chien, Y. CDR3 length in antigen-specific immune receptors. J. Exp. Med. 179, 323-328 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 323-328
    • Rock, E.P.1    Sibbald, P.R.2    Davis, M.M.3    Chien, Y.4
  • 7
    • 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. & Schmitt-Verhulst, A.-M. 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).
    • (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
  • 8
    • 0032076237 scopus 로고    scopus 로고
    • A basis for alloreactivity: MHC helical residues broaden peptide recognition by the TCR
    • Daniel, C., Horvath, S. & Alien, P. M. A basis for alloreactivity: MHC helical residues broaden peptide recognition by the TCR. Immunity 8, 543-552.
    • Immunity , vol.8 , pp. 543-552
    • Daniel, C.1    Horvath, S.2    Alien, P.M.3
  • 9
    • 0032076119 scopus 로고    scopus 로고
    • d peptide complexes
    • d peptide complexes. Immunity 8, 553-562 (1998).
    • (1998) Immunity , vol.8 , pp. 553-562
    • Speir, J.A.1
  • 10
    • 0032472057 scopus 로고    scopus 로고
    • Atomic structure of an αβ T cell receptor (TCR) heterodimer in complex with an anti-TCR Fab fragment derived from a mitogenic antibody
    • Wang, J. et al. Atomic structure of an αβ T cell receptor (TCR) heterodimer in complex with an anti-TCR Fab fragment derived from a mitogenic antibody. EMBO J. 17, 10-26 (1998).
    • (1998) EMBO J. , vol.17 , pp. 10-26
    • Wang, J.1
  • 12
    • 0031868554 scopus 로고    scopus 로고
    • Anatomy of an antibody molecule: Structure, kinetics, thermodynamics and mutational studies of the anti lysozyme antibody D1.3
    • Braden, B. C., Goldman, E. R., Mariuzza, R. A. & Poljak, R. J. Anatomy of an antibody molecule: structure, kinetics, thermodynamics and mutational studies of the anti lysozyme antibody D1.3. Immunol. Rev. 163, 45-57 (1998).
    • (1998) Immunol. Rev. , vol.163 , pp. 45-57
    • Braden, B.C.1    Goldman, E.R.2    Mariuzza, R.A.3    Poljak, R.J.4
  • 13
    • 0030935007 scopus 로고    scopus 로고
    • The MHC reactivity of the T cell repertoire prior to positive and negative selection
    • Zerrahn, J., Held, W. & Raulet, D. J. The MHC reactivity of the T cell repertoire prior to positive and negative selection. Cell 88, 627-436 (1997).
    • (1997) Cell , vol.88 , pp. 627-1436
    • Zerrahn, J.1    Held, W.2    Raulet, D.J.3
  • 14
    • 0030846879 scopus 로고    scopus 로고
    • How many thymocytes audition for selection?
    • Merkenschlager, M. et al. How many thymocytes audition for selection? J. Exp. Med. 186, 1149-1158 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1149-1158
    • Merkenschlager, M.1
  • 17
    • 0024280910 scopus 로고
    • A T cell clone expresses two T cell receptor α genes but uses one αβ heterodimer for allorecognition and self MHC-restricted antigen recognition
    • Malissen, M. et al. A T cell clone expresses two T cell receptor α genes but uses one αβ heterodimer for allorecognition and self MHC-restricted antigen recognition. Cell 55, 49-59 (1988).
    • (1988) Cell , vol.55 , pp. 49-59
    • Malissen, M.1
  • 18
    • 0000467109 scopus 로고
    • High determinant density may explain the phenomenon of alloreactivity
    • Bevan, M. J. High determinant density may explain the phenomenon of alloreactivity Immunol. Today 5, 128-130 (1984).
    • (1984) Immunol. Today , vol.5 , pp. 128-130
    • Bevan, M.J.1
  • 19
    • 0017598571 scopus 로고
    • Hypothesis: Why do so many lymphocytes respond to major histocompatibility antigens?
    • Matzinger, P. & Bevan, M. J. Hypothesis: why do so many lymphocytes respond to major histocompatibility antigens? Cell. Immunol. 29, 1-5 (1977).
    • (1977) Cell. Immunol. , vol.29 , pp. 1-5
    • Matzinger, P.1    Bevan, M.J.2
  • 20
    • 0021215441 scopus 로고
    • Interaction between MHC-encoded products and cloned T cells. II. Analyses of physiological requirements indicate two different pathways of stimulation by class 1 alloantigens
    • Albert, F., Boyer, C., Buferne, M. & Schmitt-Verhulst, A.-M. Interaction between MHC-encoded products and cloned T cells. II. Analyses of physiological requirements indicate two different pathways of stimulation by class 1 alloantigens. Immunogenetics 19, 279-294 (1984).
    • (1984) Immunogenetics , vol.19 , pp. 279-294
    • Albert, F.1    Boyer, C.2    Buferne, M.3    Schmitt-Verhulst, A.-M.4
  • 21
    • 0026531092 scopus 로고
    • Structural diversity of the classical H-2 genes: K, D, and L
    • Pullen, J. K., Horton, R. M., Cai, Z. & Pease, L. R. Structural diversity of the classical H-2 genes: K, D, and L. J. Immunol. 148, 953-967 (1992).
    • (1992) J. Immunol. , vol.148 , pp. 953-967
    • Pullen, J.K.1    Horton, R.M.2    Cai, Z.3    Pease, L.R.4
  • 22
    • 0033945378 scopus 로고    scopus 로고
    • The future of allogeneic stem cell transplantation: Minimizing pain, maximizing gain
    • Little, M. T. & Storb, R. The future of allogeneic stem cell transplantation: minimizing pain, maximizing gain. J. Clin. Invest 105, 1679-1681 (2000).
    • (2000) J. Clin. Invest , vol.105 , pp. 1679-1681
    • Little, M.T.1    Storb, R.2
  • 23
    • 0034610976 scopus 로고    scopus 로고
    • The role of peptides in T cell alloreactivity is determined by self-major histocompatibility complex molecules
    • Obst, R., Netuschil, N., Klopfer, K., Stevanovic, S. & Rammensee, H. G. The role of peptides in T cell alloreactivity is determined by self-major histocompatibility complex molecules. J. Exp. Med 191, 805-812 (2000).
    • (2000) J. Exp. Med , vol.191 , pp. 805-812
    • Obst, R.1    Netuschil, N.2    Klopfer, K.3    Stevanovic, S.4    Rammensee, H.G.5
  • 24
    • 0025816350 scopus 로고
    • Each of the two productive T cell receptor α-gene rearrangements found in both the A10 and BM3-3T cell clones give rise to an α chain which can contribute to the constitution of a surface-expressed αβ dimer
    • Couez, D., Malissen M., Buferne, M., Schmitt-Verhulst, A. M. & Malissen, B. Each of the two productive T cell receptor α-gene rearrangements found in both the A10 and BM3-3T cell clones give rise to an α chain which can contribute to the constitution of a surface-expressed αβ dimer. Int. Immunol. 3, 719-729 (1991).
    • (1991) Int. Immunol. , vol.3 , pp. 719-729
    • Couez, D.1    Malissen, M.2    Buferne, M.3    Schmitt-Verhulst, A.M.4    Malissen, B.5
  • 25
    • 0029819959 scopus 로고    scopus 로고
    • Characterization of T cell receptor single-chain Fv fragments secreted by myeloma cells
    • Grégoire, C., Malissen, B. & Mazza, G. Characterization of T cell receptor single-chain Fv fragments secreted by myeloma cells. Eur. J. Immunol. 26, 2410-2416 (1996).
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2410-2416
    • Grégoire, C.1    Malissen, B.2    Mazza, G.3
  • 26
    • 0026713069 scopus 로고
    • Crystal structure of the major histocompatibility complex class 1 H-2Kb molecule containing a single viral peptide: Implications for peptide binding and T-cell receptor recognition
    • Zhang, W., Young, A. C. M., Imarai, M., Nathenson, S. G. & Sacchettini, J. C. Crystal structure of the major histocompatibility complex class 1 H-2Kb molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition. Proc. Natl Acad. Sci. USA 89, 8403-8407 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8403-8407
    • Zhang, W.1    Young, A.C.M.2    Imarai, M.3    Nathenson, S.G.4    Sacchettini, J.C.5
  • 27
    • 0033103834 scopus 로고    scopus 로고
    • TCR binding to peptide-MHC stabilizes a flexible recognition interface
    • Willcox, B. E. et al. TCR binding to peptide-MHC stabilizes a flexible recognition interface. Immunity 10, 357-365 (1999).
    • (1999) Immunity , vol.10 , pp. 357-365
    • Willcox, B.E.1
  • 28
    • 0016434857 scopus 로고
    • Crystallization and crystal data of monellin
    • Wlodawer, A. & Hodgson, K. O. Crystallization and crystal data of monellin. Proc. Natl Acad. Sci. USA 72, 398-399 (1975).
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 398-399
    • Wlodawer, A.1    Hodgson, K.O.2
  • 29
    • 0002414103 scopus 로고
    • eds Moras, D., Podjarny, A. D. & Thierry, J. C. Oxford Univ. Press
    • Leslie, A G. W. in Crystallogrophic Computing (eds Moras, D., Podjarny, A. D. & Thierry, J. C.) 50-60 (Oxford Univ. Press, 1991).
    • (1991) Crystallogrophic Computing , pp. 50-60
    • Leslie, A.G.W.1
  • 30
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • Computational Project Number 4, CCP4
    • Computational Project Number 4, CCP4. The CCP4 Suite: Programs for Protein Crystallography. Acta Cryst. D50, 760 (1994).
    • (1994) Acta Cryst. , vol.D50 , pp. 760
  • 31
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Cryst. A50, 157-163 (1994).
    • (1994) Acta Cryst. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 32
    • 0030855425 scopus 로고    scopus 로고
    • β domain
    • β domain. EMBO J. 16, 4205-4216 (1997).
    • (1997) EMBO J. , vol.16 , pp. 4205-4216
    • Housset, D.1
  • 33
    • 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).
    • (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
  • 34
    • 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. & Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119 (1991).
    • (1991) Acta Cryst. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College London
    • Hubbard, S. J. & Thornton, J. P. "NACCESS" Computer Program, Department of Biochemistry and Molecular Biology, University College London (1993).
    • (1993) "NACCESS" Computer Program
    • Hubbard, S.J.1    Thornton, J.P.2
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Scharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Scharp, K.A.2    Honig, B.3
  • 37
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 38
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • Merrit, E. A. & Bacon, D. J. Raster 3D: photorealistic molecular graphics. Meth. Enzymol. 277, 505-524 (1997).
    • (1997) Meth. Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.