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Volumn 163, Issue 6, 1999, Pages 3286-3294

The mode of ligand recognition by two peptide:MHC class I-specific monoclonal antibodies

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MONOCLONAL ANTIBODY;

EID: 0033568295     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (27)

References (42)
  • 1
    • 0020977127 scopus 로고
    • Structural basis of antibody function
    • Davies, D. R., and H. Metzger. 1983. Structural basis of antibody function. Annu. Rev. Immunol. 1:87.
    • (1983) Annu. Rev. Immunol. , vol.1 , pp. 87
    • Davies, D.R.1    Metzger, H.2
  • 3
    • 0032078216 scopus 로고    scopus 로고
    • Quantitative aspects of T-cell recognition: From within the antigen presenting cell to within the T-cell
    • Bongrand, P., and B. Malissen, 1998. Quantitative aspects of T-cell recognition: from within the antigen presenting cell to within the T-cell. BioEssays 20:412.
    • (1998) BioEssays , vol.20 , pp. 412
    • Bongrand, P.1    Malissen, B.2
  • 6
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi, D. N., P. Ghosh, U. Utz, Q. R. Fan, W. E. Biddison, and D. C. Wiley. 1996. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384:134.
    • (1996) Nature , vol.384 , pp. 134
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 7
    • 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., K. J. Smith, D. N. Garboczi, U. Utz, W. E. Beddison, and D. C. Wiley. 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.
    • (1998) Immunity , vol.8 , pp. 403
    • Ding, Y.-H.1    Smith, K.J.2    Garboczi, D.N.3    Utz, U.4    Beddison, W.E.5    Wiley, D.C.6
  • 9
    • 0026502380 scopus 로고
    • Mapping the T cell antigen receptor/peptide contacts by variant peptide immunization of single-chain transgenics
    • Jorgensen, J. L., U. Esser, B. Fazekas de St. Groth, P. A. Reay, and M. M. Davis. 1992. Mapping the T cell antigen receptor/peptide contacts by variant peptide immunization of single-chain transgenics. Nature 355:224.
    • (1992) Nature , vol.355 , pp. 224
    • Jorgensen, J.L.1    Esser, U.2    Fazekas De St. Groth, B.3    Reay, P.A.4    Davis, M.M.5
  • 10
    • 0030855425 scopus 로고    scopus 로고
    • The three-dimensional structure of a T-cell antigen receptor VαVβ heterodimer reveals a novel arrangement of the Vβ domain
    • Housset, D., G. Mazza, C. Gregoire, C. Piras, B. Malissen, and J. C. Fontecilla-Camps. 1997. The three-dimensional structure of a T-cell antigen receptor VαVβ heterodimer reveals a novel arrangement of the Vβ domain. EMBO J. 15:4205.
    • (1997) EMBO J. , vol.15 , pp. 4205
    • Housset, D.1    Mazza, G.2    Gregoire, C.3    Piras, C.4    Malissen, B.5    Fontecilla-Camps, J.C.6
  • 13
    • 0025964038 scopus 로고
    • Structure, function and properties of antibody binding sites
    • Mian, S., A. R. Bradwell, and A. J. Olson. 1991. Structure, function and properties of antibody binding sites. J. Mol. Biol. 217:133.
    • (1991) J. Mol. Biol. , vol.217 , pp. 133
    • Mian, S.1    Bradwell, A.R.2    Olson, A.J.3
  • 15
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan, E. 1994. Anatomy of the antibody molecule. Mol. Immunol. 31:169.
    • (1994) Mol. Immunol. , vol.31 , pp. 169
    • Padlan, E.1
  • 17
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • MacCallum, R. M., A. C. R. Martin, and J. M. Thorton. 1996. Antibody-antigen interactions: contact analysis and binding site topography. J. Mol. Biol. 262:732.
    • (1996) J. Mol. Biol. , vol.262 , pp. 732
    • MacCallum, R.M.1    Martin, A.C.R.2    Thorton, J.M.3
  • 18
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide:MHC antigen
    • Garcia, K. C., M. Deagno, L. R. Pease, M. Huang, P. A. Peterson, L. Teyton, and I. A. Wilson. 1998. Structural basis of plasticity in T cell receptor recognition of a self peptide:MHC antigen. Science 279:1166.
    • (1998) Science , vol.279 , pp. 1166
    • Garcia, K.C.1    Deagno, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5    Teyton, L.6    Wilson, I.A.7
  • 20
    • 0028518986 scopus 로고
    • Intracellular assembly and transport of endogenous peptide-MHC class II complexes
    • Rudensky, A. Y., M. Maric, S. Eastman, L. Shoemaker, P. C. DeRoos, and J. S. Blum. 1994. Intracellular assembly and transport of endogenous peptide-MHC class II complexes. Immunity 1:585.
    • (1994) Immunity , vol.1 , pp. 585
    • Rudensky, A.Y.1    Maric, M.2    Eastman, S.3    Shoemaker, L.4    DeRoos, P.C.5    Blum, J.S.6
  • 21
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody
    • Porgador, A., J. W. Yewdell, Y. Deng, J. R. Bennink, and R. N. Germain. 1997. Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity 6:715.
    • (1997) Immunity , vol.6 , pp. 715
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5
  • 22
    • 0027435989 scopus 로고
    • Peptide variants reveal how antibodies recognize major histocompatibility complex class I
    • Hogquist, K. A., A. G. Grandea, and M. J. Bevan. 1993. Peptide variants reveal how antibodies recognize major histocompatibility complex class I. Eur. J. Immunol. 23:3028.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 3028
    • Hogquist, K.A.1    Grandea, A.G.2    Bevan, M.J.3
  • 23
    • 0025006862 scopus 로고
    • Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro
    • M
    • Schumacher, N. M., M.-T. Heemels, J. J. Neefjes, W. M. Kast, C. J. Melief, M., and H. L. Ploegh. 1990. Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro. Cell 62:563.
    • (1990) Cell , vol.62 , pp. 563
    • Schumacher, N.M.1    Heemels, M.-T.2    Neefjes, J.J.3    Kast, W.M.4    Melief, C.J.5    Ploegh, H.L.6
  • 24
    • 0030018187 scopus 로고    scopus 로고
    • T-cell receptor (TCR) recognition of MHC class I variant: Intermolecular second site reversion provides evidence for peptide:MHC conformational variation
    • Dyall, R., D. H. Fremont, C. S. Jameson, and J. Nikolic-Zugic. 1996. T-cell receptor (TCR) recognition of MHC class I variant: intermolecular second site reversion provides evidence for peptide:MHC conformational variation. J. Exp. Med. 184:253.
    • (1996) J. Exp. Med. , vol.184 , pp. 253
    • Dyall, R.1    Fremont, D.H.2    Jameson, C.S.3    Nikolic-Zugic, J.4
  • 26
    • 0030734053 scopus 로고    scopus 로고
    • The critical role of a solvent-exposed residue of an MHC class I-restricted peptide in MHC-peptide binding
    • Huard, R., R. Dyall, and J. Nikolic-Zugic. 1997. The critical role of a solvent-exposed residue of an MHC class I-restricted peptide in MHC-peptide binding. Int. Immunol. 9:1701.
    • (1997) Int. Immunol. , vol.9 , pp. 1701
    • Huard, R.1    Dyall, R.2    Nikolic-Zugic, J.3
  • 29
    • 0022568243 scopus 로고
    • Murine major histocompatibility complex class I mutants: Molecular analysis and structure-function implications
    • Nathenson, S. G., J. Geliebter, G. M. Pfaffenbach, and R. A. Zeff. 1986. Murine major histocompatibility complex class I mutants: molecular analysis and structure-function implications. Annu. Rev. Immunol. 4:471.
    • (1986) Annu. Rev. Immunol. , vol.4 , pp. 471
    • Nathenson, S.G.1    Geliebter, J.2    Pfaffenbach, G.M.3    Zeff, R.A.4
  • 30
    • 0028987213 scopus 로고
    • b-ovalbumin peptide complexes reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove
    • b-ovalbumin peptide complexes reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl. Acad. Sci. USA 92:2479.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2479
    • Fremont, D.H.1    Stura, E.A.2    Masazumi, M.3    Peterson, P.A.4    Wilson, I.A.5
  • 31
    • 0025021670 scopus 로고
    • Role of self-peptides in positively selecting the T-cell repertoire
    • Nikolic-Zugic, J., and M. J. Bevan. 1990. Role of self-peptides in positively selecting the T-cell repertoire. Nature 344:65.
    • (1990) Nature , vol.344 , pp. 65
    • Nikolic-Zugic, J.1    Bevan, M.J.2
  • 32
    • 0023187442 scopus 로고
    • The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
    • Bjorkman, P. J., M. A. Saper, B. Samraoui, W. S. Bennett, J. L. Strominger, and D. C. Wiley. 1987. The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature 329:512.
    • (1987) Nature , vol.329 , pp. 512
    • Bjorkman, P.J.1    Saper, M.A.2    Samraoui, B.3    Bennett, W.S.4    Strominger, J.L.5    Wiley, D.C.6
  • 33
    • 0024420425 scopus 로고
    • The functional significance of two amino acid polymorphisms in the antigen binding domain of class I MHC molecules
    • Pullen, J. K., H. D. Hunt, R. M. Horton, and L. R. Pease. 1989. The functional significance of two amino acid polymorphisms in the antigen binding domain of class I MHC molecules. J. Immunol. 143:1674.
    • (1989) J. Immunol. , vol.143 , pp. 1674
    • Pullen, J.K.1    Hunt, H.D.2    Horton, R.M.3    Pease, L.R.4
  • 34
    • 0031229844 scopus 로고    scopus 로고
    • b-restricted ovalbumin peptide suggests that the β-chain subunit can dominate the determination of peptide side chain specificity
    • b-restricted ovalbumin peptide suggests that the β-chain subunit can dominate the determination of peptide side chain specificity. J. Immunol 159:2312.
    • (1997) J. Immunol , vol.159 , pp. 2312
    • Turner, S.J.1    Jameson, J.C.2    Carbone, F.R.3
  • 35
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk, K., O. Rotzschke, S. Stevanovic, G. Jung, and H.-G. Rammensee. 1991. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351:290.
    • (1991) Nature , vol.351 , pp. 290
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 36
    • 0027533676 scopus 로고
    • Changes at peptide residues buried in the major histocompatibility complex (MHC) class I binding cleft influence T cell recognition: A possible role for indirect conformational alterations in the MHC class I or bound peptide in determining T cell recognition
    • Chen, W., J. McCluskey, S. Rodda, and F. R. Carbone. 1993. Changes at peptide residues buried in the major histocompatibility complex (MHC) class I binding cleft influence T cell recognition: a possible role for indirect conformational alterations in the MHC class I or bound peptide in determining T cell recognition. J. Exp. Med. 177:869.
    • (1993) J. Exp. Med. , vol.177 , pp. 869
    • Chen, W.1    McCluskey, J.2    Rodda, S.3    Carbone, F.R.4
  • 37
    • 0028123440 scopus 로고
    • Conformational differences in major histocompatibility complex-peptide complexes can result in alloreactivity
    • Chattopadhyay, S., T. Matthias, J. Biggs, and L. A. Sherman. 1994. Conformational differences in major histocompatibility complex-peptide complexes can result in alloreactivity. J. Exp. Med. 179:213.
    • (1994) J. Exp. Med. , vol.179 , pp. 213
    • Chattopadhyay, S.1    Matthias, T.2    Biggs, J.3    Sherman, L.A.4
  • 40
    • 0027443107 scopus 로고
    • Identification of conserved T cell receptor CDR3 residues contacting known exposed peptide side chains from a major histocompatibility complex class I-bound determinant
    • Kelly, J. M., S. J. Sterry, S. Cose, S. J. Turner, S. Rodda, P. J. Fink, and F. R. Carbone. 1993. Identification of conserved T cell receptor CDR3 residues contacting known exposed peptide side chains from a major histocompatibility complex class I-bound determinant. Eur. J. Immunol. 23:3318.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 3318
    • Kelly, J.M.1    Sterry, S.J.2    Cose, S.3    Turner, S.J.4    Rodda, S.5    Fink, P.J.6    Carbone, F.R.7
  • 41
    • 0023748578 scopus 로고
    • Evidence that multiple residues on both the α-helices of the class I MHC molecule are simultaneously recognized by the T cell receptor
    • Ajitkumar, P., S. S. Geier, K. V. Kesari, F. Borriello, M. Nakagawa, J. A. Bluestone, M. A. Saper, D. C. Wiley, and S. G. Natheson. 1988. Evidence that multiple residues on both the α-helices of the class I MHC molecule are simultaneously recognized by the T cell receptor. Cell 54:47.
    • (1988) Cell , vol.54 , pp. 47
    • Ajitkumar, P.1    Geier, S.S.2    Kesari, K.V.3    Borriello, F.4    Nakagawa, M.5    Bluestone, J.A.6    Saper, M.A.7    Wiley, D.C.8    Natheson, S.G.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.