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Volumn 285, Issue 2, 1999, Pages 645-653

Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus

Author keywords

Crystal structure; Epstein Barr virus; HLA class I molecules; Peptide conformation; Peptide termini positioning

Indexed keywords

HLA B ANTIGEN; NEF PROTEIN; PEPTIDE;

EID: 0033556246     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2363     Document Type: Article
Times cited : (47)

References (35)
  • 2
    • 0025324091 scopus 로고
    • Structure, function and diversity of class I major histocompatibility complex molecules
    • Bjorkman P. J., Parham P. Structure, function and diversity of class I major histocompatibility complex molecules. Annu. Rev. Biochem. 59:1990;253-288.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 253-288
    • Bjorkman, P.J.1    Parham, P.2
  • 4
    • 0003769049 scopus 로고
    • New Haven and London: Yale University Press
    • Brünger A. T. X-PLOR Version 3.1. 1992a;Yale University Press, New Haven and London.
    • (1992) X-PLOR Version 3.1
    • Brünger, A.T.1
  • 5
    • 0026597444 scopus 로고
    • The free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A. T. The free R-value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992b;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Ccp4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 9
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 10
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representation of macromolecules
    • Evans S. V. SETOR: hardware lighted three-dimensional solid model representation of macromolecules. J. Mol. Graph. 11:1993;134-138.
    • (1993) J. Mol. Graph , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 11
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk K., Rötzschke O., Stevanovic S., Jung G., Rammensee H.-G. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature. 351:1991;290-296.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rötzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 13
    • 0030931534 scopus 로고    scopus 로고
    • Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors
    • Fan Q. R., Mosyak L., Winter C. C., Wagtmann N., Long E. O., Wiley D. C. Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors. Nature. 389:1997;96-100.
    • (1997) Nature , vol.389 , pp. 96-100
    • Fan, Q.R.1    Mosyak, L.2    Winter, C.C.3    Wagtmann, N.4    Long, E.O.5    Wiley, D.C.6
  • 15
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
    • Garboczi D. N., Hung D. T., Wiley D. C. HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proc. Natl Acad. Sci USA. 89:1992;3429-3433.
    • (1992) Proc. Natl Acad. Sci USA , vol.89 , pp. 3429-3433
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 16
    • 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., Wiley D. C. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature. 384:1996;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
  • 17
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia K. C., Degano M., Pease L. R., Huang M., Peterson P. A., Teyton L., Wilson I. A. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science. 279:1998;1166-1172.
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1    Degano, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5    Teyton, L.6    Wilson, I.A.7
  • 21
    • 0022333120 scopus 로고
    • Diffraction methods for biological macromolecules: Interactive computer graphics: FRODO
    • Jones T. A. Diffraction methods for biological macromolecules: interactive computer graphics: FRODO. Methods Enzymol. 115:1985;157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 22
    • 0028908939 scopus 로고
    • Epstein-Barr virus isolates with the major HLA B35. 01-restricted cytotoxic T lymphocyte epitope are prevalent in a highly B35. 01-positive African population
    • Lee S. P., Morgan S., Skinner J., Thomas W. A., Jones S. R., Sutton J., Khanna R., Whittle H. C., Rickinson A. B. Epstein-Barr virus isolates with the major HLA B35. 01-restricted cytotoxic T lymphocyte epitope are prevalent in a highly B35. 01-positive African population. Eur. J. Immuol. 25:1995;102-110.
    • (1995) Eur. J. Immuol. , vol.25 , pp. 102-110
    • Lee, S.P.1    Morgan, S.2    Skinner, J.3    Thomas, W.A.4    Jones, S.R.5    Sutton, J.6    Khanna, R.7    Whittle, H.C.8    Rickinson, A.B.9
  • 23
    • 0028888835 scopus 로고
    • Dengue virus-specific, HLA-B35-restricted, human CD8+ cytotoxic T lymphocytes (CTL) clones. Recognition of NS3 amino acids 500 to 508 by CTL clones of two different serotype specificities
    • Livingston P. G., Kurane I., Dai L. C., Okamoto Y., Lai C. J., Men R., Karaki S., Takiguchi M., Ennis F. A. Dengue virus-specific, HLA-B35-restricted, human CD8+ cytotoxic T lymphocytes (CTL) clones. Recognition of NS3 amino acids 500 to 508 by CTL clones of two different serotype specificities. J. Immunol. 154:1995;1287-1295.
    • (1995) J. Immunol. , vol.154 , pp. 1287-1295
    • Livingston, P.G.1    Kurane, I.2    Dai, L.C.3    Okamoto, Y.4    Lai, C.J.5    Men, R.6    Karaki, S.7    Takiguchi, M.8    Ennis, F.A.9
  • 24
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden D. R., Gorga J. C., Strominger J. L., Wiley D. C. The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell. 70:1992;1035-1048.
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 25
    • 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. N., Wiley D. C. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell. 75:1993;693-708.
    • (1993) Cell , vol.75 , pp. 693-708
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 27
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 28
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington: SERC Daresbury Laboratory
    • Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend: Data Collection and Processing. 1993;56-62 SERC Daresbury Laboratory, Warrington.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 31
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
    • Saper M. A., Bjorkman P. J., Wiley D. C. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219:1991;277-319.
    • (1991) J. Mol. Biol. , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 32
    • 0026621224 scopus 로고
    • Atomic structure of a human MHC molecule presenting an influenza virus peptide
    • Silver M. L., Guo H.-C., Strominger J. L., Wiley D. C. Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature. 360:1992;367-369.
    • (1992) Nature , vol.360 , pp. 367-369
    • Silver, M.L.1    Guo, H.-C.2    Strominger, J.L.3    Wiley, D.C.4
  • 33
    • 0029969665 scopus 로고    scopus 로고
    • Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53
    • Smith K. J., Reid S. W., Harlos K., McMichael A. J., Stuart D. I., Bell J. I., Jones E. Y. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity. 4:1996a;215-228.
    • (1996) Immunity , vol.4 , pp. 215-228
    • Smith, K.J.1    Reid, S.W.2    Harlos, K.3    McMichael, A.J.4    Stuart, D.I.5    Bell, J.I.6    Jones, E.Y.7
  • 35
    • 0027411509 scopus 로고
    • Soluble T cell receptor-like properties of an HLA-B35-specific monoclonal antibody (TÜ165)
    • Uchanska-Ziegler B., Nößner E., Schenk A., Ziegler A., Schendel D. J. Soluble T cell receptor-like properties of an HLA-B35-specific monoclonal antibody (TÜ165). Eur. J. Immunol. 23:1993;734-738.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 734-738
    • Uchanska-Ziegler, B.1    Nößner, E.2    Schenk, A.3    Ziegler, A.4    Schendel, D.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.