메뉴 건너뛰기




Volumn 387, Issue 6632, 1997, Pages 527-530

Dimeric association and segmental variability in the structure of human CD4

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN;

EID: 0030911709     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/387527a0     Document Type: Article
Times cited : (246)

References (29)
  • 1
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A. & Littman, D. R. Signal transduction by lymphocyte antigen receptors. Cell 76, 263-274 (1994).
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 2
    • 0024474326 scopus 로고
    • Role of CD4 in normal immunity and HIV infection
    • Lifson, J. D. & Engleman, E. G. Role of CD4 in normal immunity and HIV infection. Immunol. Rev. 109, 93-117 (1989).
    • (1989) Immunol. Rev. , vol.109 , pp. 93-117
    • Lifson, J.D.1    Engleman, E.G.2
  • 3
    • 0023845937 scopus 로고
    • A soluble form of CD4 (T4) protein inhibits AIDS virus infection
    • Deen, K. C. et al. A soluble form of CD4 (T4) protein inhibits AIDS virus infection. Nature 331, 82-84 (1988).
    • (1988) Nature , vol.331 , pp. 82-84
    • Deen, K.C.1
  • 4
    • 0025004265 scopus 로고
    • Molecular characteristics of recombinant human CD4 as deduced from polymorphic crystals
    • Kwong, P. D. et al. Molecular characteristics of recombinant human CD4 as deduced from polymorphic crystals. Proc. Natl Acad. Sci. USA 87, 6423-6427 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 6423-6427
    • Kwong, P.D.1
  • 5
    • 0025224767 scopus 로고
    • Crystal structure of an HIV-binding recombinant fragment of human CD4
    • Ryu, S.-E. et al. Crystal structure of an HIV-binding recombinant fragment of human CD4 Nature 348, 419-426 (1990).
    • (1990) Nature , vol.348 , pp. 419-426
    • Ryu, S.-E.1
  • 6
    • 0025198478 scopus 로고
    • Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains
    • Wang, J. et al. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature 348 411-418 (1990).
    • (1990) Nature , vol.348 , pp. 411-418
    • Wang, J.1
  • 7
    • 0027219115 scopus 로고
    • Crystal structure of domains 3 and 4 of rat CD4: Relation to the NH2-terminal domains
    • Brady, R. L. et al. Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains. Science 260, 979-983 (1993).
    • (1993) Science , vol.260 , pp. 979-983
    • Brady, R.L.1
  • 8
    • 0001632513 scopus 로고    scopus 로고
    • Combined molecular replacement
    • Tong, L. Combined molecular replacement. Acta Crystallogr. A 52, 782-784 (1996).
    • (1996) Acta Crystallogr. A , vol.52 , pp. 782-784
    • Tong, L.1
  • 9
    • 0028177807 scopus 로고
    • Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices
    • Ryu, S.-E., Truneh, A., Sweet, R. W. & Hendrickson, W. A. Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices. Structure 2, 59-74 (1994).
    • (1994) Structure , vol.2 , pp. 59-74
    • Ryu, S.-E.1    Truneh, A.2    Sweet, R.W.3    Hendrickson, W.A.4
  • 10
    • 0025949829 scopus 로고
    • Mutational analysis of the interaction between CD4 and class II MHC: Class II antigen contact CD4 on a surface opposite the gp120-binding site
    • Fleury, S. et al. Mutational analysis of the interaction between CD4 and class II MHC: class II antigen contact CD4 on a surface opposite the gp120-binding site. Cell 66, 1037-1049 (1991).
    • (1991) Cell , vol.66 , pp. 1037-1049
    • Fleury, S.1
  • 11
    • 0029071074 scopus 로고
    • Oligomerization of CD4 is required for stable binding to class II major histocompatibility complex proteins but not for interaction with human immunodeficiency virus go120
    • Sakihama, T., Smolyar, A. & Reinherz, E. L. Oligomerization of CD4 is required for stable binding to class II major histocompatibility complex proteins but not for interaction with human immunodeficiency virus go120. Proc. Natl Acad. Sci. USA 92, 6444-6448 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6444-6448
    • Sakihama, T.1    Smolyar, A.2    Reinherz, E.L.3
  • 12
    • 0029150969 scopus 로고
    • Involvement of both major histocompatibility complex class II alpha and beta chains in CD4 function indicates a role for ordered oligomerization in T-cell activation
    • König, R., Shen, X. & Germain, R. N. Involvement of both major histocompatibility complex class II alpha and beta chains in CD4 function indicates a role for ordered oligomerization in T-cell activation. J. Exp. Med. 182, 779-787 (1995).
    • (1995) J. Exp. Med. , vol.182 , pp. 779-787
    • König, R.1    Shen, X.2    Germain, R.N.3
  • 13
    • 0027049402 scopus 로고
    • Human immunodeficiency virus gp120 binding C′C″ ridge of CD4 domain 1 is also involved in interaction with class II major histocompatibility complex molecules
    • Moebius, U. et al. Human immunodeficiency virus gp120 binding C′C″ ridge of CD4 domain 1 is also involved in interaction with class II major histocompatibility complex molecules. Immunology 89, 12008-12012 (1992).
    • (1992) Immunology , vol.89 , pp. 12008-12012
    • Moebius, U.1
  • 14
    • 0027171292 scopus 로고
    • Delineation of an extended surface area on human CD4 involved in class II major histocompatibility complex binding
    • Moebius, U., Pallai, P., Harrison, S. C. & Reinherz, E. L. Delineation of an extended surface area on human CD4 involved in class II major histocompatibility complex binding. Proc. Natl Acad. Sci. USA 90, 8259-8263 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8259-8263
    • Moebius, U.1    Pallai, P.2    Harrison, S.C.3    Reinherz, E.L.4
  • 15
    • 0030638941 scopus 로고    scopus 로고
    • Analysis of the contact sites on the CD4 molecule with class II MHC molecule: Co-ligand versus co-receptor function
    • Huang, G., Fleury, S., Yachou, A., Hendrickson, W. A. & Sekaly, R. Analysis of the contact sites on the CD4 molecule with class II MHC molecule: co-ligand versus co-receptor function. J. Immunol. 158, 216-225 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 216-225
    • Huang, G.1    Fleury, S.2    Yachou, A.3    Hendrickson, W.A.4    Sekaly, R.5
  • 16
    • 0029848952 scopus 로고    scopus 로고
    • Postbinding events mediated by human immunodeficiency virus type I are sensitive to modifications in the D4-transmembrane linked region of CD4
    • Moir, S., Perreault, J. & Poulin, L. Postbinding events mediated by human immunodeficiency virus type I are sensitive to modifications in the D4-transmembrane linked region of CD4. J. Virol. 70, 8019-8028 (1996).
    • (1996) J. Virol. , vol.70 , pp. 8019-8028
    • Moir, S.1    Perreault, J.2    Poulin, L.3
  • 17
    • 0025176060 scopus 로고
    • Novel anti-CD4 monoclonal antibodies separate human immunodeficiency virus infection and fusion of CD4+ cells from virus binding
    • Healey, D. et al. Novel anti-CD4 monoclonal antibodies separate human immunodeficiency virus infection and fusion of CD4+ cells from virus binding. J. Exp. Med. 172, 1233-1242 (1990).
    • (1990) J. Exp. Med. , vol.172 , pp. 1233-1242
    • Healey, D.1
  • 18
    • 0029805881 scopus 로고    scopus 로고
    • Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines
    • Lapham, C. K. et al. Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines. Science 274, 602-605 (1996).
    • (1996) Science , vol.274 , pp. 602-605
    • Lapham, C.K.1
  • 19
    • 16144365650 scopus 로고    scopus 로고
    • CD4-induced interaction of primary HFV-1 gp120 glycoproteins with the chemokine receptor CCR-5
    • Wu, L. et al. CD4-induced interaction of primary HFV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature, 384 179-183 (1996).
    • (1996) Nature , vol.384 , pp. 179-183
    • Wu, L.1
  • 20
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A. & Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell 61, 203-212 (1990).
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 21
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase kk upon tyrosine phosphorylation
    • Yamaguchi, H. & Hendrickson, W. A. Structural basis for activation of human lymphocyte kinase kk upon tyrosine phosphorylation. Nature 384, 484-489 (1996).
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 22
    • 0023387490 scopus 로고
    • Coclustering of CD4 (L3T4) molecule with the T-cell receptor is induced by specific direct interaction of helper T cells and antigen-presenting cells
    • Kupfer, A., Singer, S. J., Janeway, C. A. & Swain, S. L. Coclustering of CD4 (L3T4) molecule with the T-cell receptor is induced by specific direct interaction of helper T cells and antigen-presenting cells. Proc. Natl Acad. Sci. USA 84, 5888-5892 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5888-5892
    • Kupfer, A.1    Singer, S.J.2    Janeway, C.A.3    Swain, S.L.4
  • 23
    • 0028485771 scopus 로고
    • Volume-specific amino acid analysis: A method for Za determination
    • Kwong, P. D., Pound, A. & Hendrickson, W. A. Volume-specific amino acid analysis: a method for Za determination. J. Appl. Crystallogr. 27, 504-509 (1994).
    • (1994) J. Appl. Crystallogr. , vol.27 , pp. 504-509
    • Kwong, P.D.1    Pound, A.2    Hendrickson, W.A.3
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in those models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building models in electron density maps and the location of errors in those models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0027969548 scopus 로고
    • Determination of diffusion coefficients of biological macromolecules by dynamic light scattering
    • Harding, S. E. Determination of diffusion coefficients of biological macromolecules by dynamic light scattering. Methods Mol. Biol. 22, 97-108 (1994).
    • (1994) Methods Mol. Biol. , vol.22 , pp. 97-108
    • Harding, S.E.1
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. 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.1
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 29
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans, S. V. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 111, 134-138 (1993).
    • (1993) J. Mol. Graph. , vol.111 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.