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Volumn 163, Issue , 1998, Pages 217-236

CD2 and the nature of protein interactions mediating cell-cell recognition

Author keywords

[No Author keywords available]

Indexed keywords

CD2 ANTIGEN;

EID: 0031817313     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1998.tb01199.x     Document Type: Review
Times cited : (120)

References (102)
  • 1
    • 0017584586 scopus 로고
    • Analysis of cell surfaces by xenogeneic myeloma-hybrid antibodies: Differentiation antigens of rat lymphocytes
    • Williams AF, Galfre G, Milstein C. Analysis of cell surfaces by xenogeneic myeloma-hybrid antibodies: differentiation antigens of rat lymphocytes. Cell 1977;12:663-673.
    • (1977) Cell , vol.12 , pp. 663-673
    • Williams, A.F.1    Galfre, G.2    Milstein, C.3
  • 6
    • 0025198478 scopus 로고
    • Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains
    • Wang JH, et al. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature 1990;348:411-418.
    • (1990) Nature , vol.348 , pp. 411-418
    • Wang, J.H.1
  • 7
    • 0025224767 scopus 로고
    • Crystal structure of an HIV-binding recombinant fragment of human CD4
    • Ryu SE, et al. Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature 1990;348:419-426.
    • (1990) Nature , vol.348 , pp. 419-426
    • Ryu, S.E.1
  • 8
    • 0029930984 scopus 로고    scopus 로고
    • The structure and ligand interactions of CD2: Implications for T-cell function
    • Davis SJ, van der Merwe PA. The structure and ligand interactions of CD2: implications for T-cell function. Immunol Today 1996;17:177-187.
    • (1996) Immunol Today , vol.17 , pp. 177-187
    • Davis, S.J.1    Van Der Merwe, P.A.2
  • 9
    • 0023069478 scopus 로고
    • The lymphocyte function-associated LFA-1, CD2, and LFA-3 molecules: Cell adhesion receptors of the immune system
    • Springer TA, Dustin ML, Kishimoto TK, Marlin SD. The lymphocyte function-associated LFA-1, CD2, and LFA-3 molecules: cell adhesion receptors of the immune system. Annu Rev Immunol 1987;5:223-252.
    • (1987) Annu Rev Immunol , vol.5 , pp. 223-252
    • Springer, T.A.1    Dustin, M.L.2    Kishimoto, T.K.3    Marlin, S.D.4
  • 11
    • 0024472149 scopus 로고
    • The structural biology of CD2
    • Moingeon P, et al. The structural biology of CD2. Immunol Rev 1989;111:111-144.
    • (1989) Immunol Rev , vol.111 , pp. 111-144
    • Moingeon, P.1
  • 12
    • 0022360904 scopus 로고
    • The cell surface molecule recognized by the erythrocyte receptor of T lymphocytes. Identification and partial characterization using a monoclonal antibody
    • Hunig T. The cell surface molecule recognized by the erythrocyte receptor of T lymphocytes. Identification and partial characterization using a monoclonal antibody. J Exp Med 1985;162:890-901.
    • (1985) J Exp Med , vol.162 , pp. 890-901
    • Hunig, T.1
  • 14
    • 0023238643 scopus 로고
    • Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes
    • Sayre PH, et al. Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes. Proc Natl Acad Sci USA 1987;84:2941-2945.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2941-2945
    • Sayre, P.H.1
  • 15
    • 0000820364 scopus 로고
    • Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure
    • Seed B, Aruffo A. Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. Proc Natl Acad Sci USA 1987;84:3365-3369.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3365-3369
    • Seed, B.1    Aruffo, A.2
  • 16
    • 0023637186 scopus 로고
    • An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2
    • Seed B. An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2. Nature 1987;329:840-842.
    • (1987) Nature , vol.329 , pp. 840-842
    • Seed, B.1
  • 17
    • 0023544493 scopus 로고
    • Primary structure of lymphocyte function-associated antigen 3 (LFA-3). The ligand of the T lymphocyte CD2 glycoprotein
    • Wallner BP, et al. Primary structure of lymphocyte function-associated antigen 3 (LFA-3). The ligand of the T lymphocyte CD2 glycoprotein. J Exp Med 1987;166:923-932.
    • (1987) J Exp Med , vol.166 , pp. 923-932
    • Wallner, B.P.1
  • 18
    • 0024095774 scopus 로고
    • The MRC OX-45 antigen of rat leukocytes and endothelium is in a subset of the immunoglobulin superfamily with CD2, LFA-3 and carcinoembryonic antigens
    • Killeen N, Moessner R, Arvieux J, Willis A, Williams AF. The MRC OX-45 antigen of rat leukocytes and endothelium is in a subset of the immunoglobulin superfamily with CD2, LFA-3 and carcinoembryonic antigens. EMBO J 1988;7:3087-3091.
    • (1988) EMBO J , vol.7 , pp. 3087-3091
    • Killeen, N.1    Moessner, R.2    Arvieux, J.3    Willis, A.4    Williams, A.F.5
  • 19
    • 0023767124 scopus 로고
    • The human LFA-3 gene is located at the same chromosome band as the gene for its receptor CD2
    • Sewell WA, et al. The human LFA-3 gene is located at the same chromosome band as the gene for its receptor CD2. Immunogenetics 1988;28:278-282.
    • (1988) Immunogenetics , vol.28 , pp. 278-282
    • Sewell, W.A.1
  • 20
    • 0024393729 scopus 로고
    • Physical linkage of genes encoding the lymphocyte adhesion molecules CD2 and its ligand LFA-3
    • Kingsmore SF, Watson ML, Moseley WS, Seldin MF. Physical linkage of genes encoding the lymphocyte adhesion molecules CD2 and its ligand LFA-3. Immunogenetics 1989;30:123-125.
    • (1989) Immunogenetics , vol.30 , pp. 123-125
    • Kingsmore, S.F.1    Watson, M.L.2    Moseley, W.S.3    Seldin, M.F.4
  • 21
    • 0025293056 scopus 로고
    • Structure, expression, and genetic linkage of the mouse BCM1 (OX45 or Blast-1) antigen. Evidence for genetic duplication giving rise to the BCM1 region on mouse chromosome 1 and the CD2/LFA3 region on mouse chromosome 3
    • Wong YW, Williams AF, Kingsmore SF, Seldin MF. Structure, expression, and genetic linkage of the mouse BCM1 (OX45 or Blast-1) antigen. Evidence for genetic duplication giving rise to the BCM1 region on mouse chromosome 1 and the CD2/LFA3 region on mouse chromosome 3. J Exp Med 1990;171:2115-2130.
    • (1990) J Exp Med , vol.171 , pp. 2115-2130
    • Wong, Y.W.1    Williams, A.F.2    Kingsmore, S.F.3    Seldin, M.F.4
  • 22
    • 0026667450 scopus 로고
    • CD48 is a counter-receptor for mouse CD2 and is involved in T cell activation
    • Kato K, et al. CD48 is a counter-receptor for mouse CD2 and is involved in T cell activation. J Exp Med 1992;176:1241-1249.
    • (1992) J Exp Med , vol.176 , pp. 1241-1249
    • Kato, K.1
  • 23
    • 0027335789 scopus 로고
    • 2-terminal domain of rat CD2 binds rat CD48 with a low affinity and binding does not require glycosylation of CD2
    • 2-terminal domain of rat CD2 binds rat CD48 with a low affinity and binding does not require glycosylation of CD2. Eur J Immunol 1993;23:1373-1377.
    • (1993) Eur J Immunol , vol.23 , pp. 1373-1377
    • Van Der Merwe, P.A.1
  • 24
    • 0027405371 scopus 로고
    • A soluble multimeric recombinant CD2 protein identifies CD48 as a low affinity ligand for human CD2: Divergence of CD2 ligands during the evolution of humans and mice
    • Arulanandam AR, et al. A soluble multimeric recombinant CD2 protein identifies CD48 as a low affinity ligand for human CD2: divergence of CD2 ligands during the evolution of humans and mice. J Exp Med 1993;177:1439-1450.
    • (1993) J Exp Med , vol.177 , pp. 1439-1450
    • Arulanandam, A.R.1
  • 25
    • 0026704425 scopus 로고
    • Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59
    • Hahn WC, Menu E, Bothwell AL, Sims PJ, Bierer BE. Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59. Science 1992;256:1805-1807.
    • (1992) Science , vol.256 , pp. 1805-1807
    • Hahn, W.C.1    Menu, E.2    Bothwell, A.L.3    Sims, P.J.4    Bierer, B.E.5
  • 26
    • 0027932728 scopus 로고
    • Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59
    • Van der Merwe PA, et al. Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59. Biochemistry 1994;33:10149-10160.
    • (1994) Biochemistry , vol.33 , pp. 10149-10160
    • Van Der Merwe, P.A.1
  • 27
    • 0026478567 scopus 로고
    • Development and function of T cells in mice with a disrupted CD2 gene
    • Killeen N, Stuart SG, Littman DR. Development and function of T cells in mice with a disrupted CD2 gene. EMBO J 1992;11:4329-4336.
    • (1992) EMBO J , vol.11 , pp. 4329-4336
    • Killeen, N.1    Stuart, S.G.2    Littman, D.R.3
  • 30
    • 0027977974 scopus 로고
    • Transient intercellular adhesion: The importance of weak protein-protein interactions
    • Van der Merwe PA, Barclay AN. Transient intercellular adhesion: the importance of weak protein-protein interactions. Trends Biochem Sci 1994;19:354-358.
    • (1994) Trends Biochem Sci , vol.19 , pp. 354-358
    • Van Der Merwe, P.A.1    Barclay, A.N.2
  • 31
    • 0027500841 scopus 로고
    • Affinity and kinetic analysis of the interaction of the cell-adhesion molecules rat CD2 and CD48
    • Van der Merwe PA, Brown MH, Davis SJ, Barclay AN. Affinity and kinetic analysis of the interaction of the cell-adhesion molecules rat CD2 and CD48. EMBO J 1993;12:4945-4954.
    • (1993) EMBO J , vol.12 , pp. 4945-4954
    • Van Der Merwe, P.A.1    Brown, M.H.2    Davis, S.J.3    Barclay, A.N.4
  • 32
    • 0031054242 scopus 로고    scopus 로고
    • CD80 (B7-1) binds both CD28 and CTLA-4 with a low affinity and very fast kinetics
    • Van der Merwe PA, Bodian DL, Daenke S, Linsley P, Davis SJ. CD80 (B7-1) binds both CD28 and CTLA-4 with a low affinity and very fast kinetics. J Exp Med 1997;185:393-403.
    • (1997) J Exp Med , vol.185 , pp. 393-403
    • Van Der Merwe, P.A.1    Bodian, D.L.2    Daenke, S.3    Linsley, P.4    Davis, S.J.5
  • 34
    • 0030448942 scopus 로고
    • Determination of the life-time and force dependence of interactions of single bonds between surface-attached CD2 and CD48 adhesion molecules
    • Pierres A, Benoliel AM, Bongrand P, van der Merwe PA. Determination of the life-time and force dependence of interactions of single bonds between surface-attached CD2 and CD48 adhesion molecules. Proc Natl Acad Sci USA 1994;93: 15114-15118.
    • (1994) Proc Natl Acad Sci USA , vol.93 , pp. 15114-15118
    • Pierres, A.1    Benoliel, A.M.2    Bongrand, P.3    Van Der Merwe, P.A.4
  • 35
    • 0031055273 scopus 로고    scopus 로고
    • The dependence of the association rate of surface-attached adhesion molecules CD2 and CD48 on separation distance
    • Pierres A, Benoliel AM, Bongrand P, van der Merwe PA. The dependence of the association rate of surface-attached adhesion molecules CD2 and CD48 on separation distance. FEBS Lett 1997;403:239-244.
    • (1997) FEBS Lett , vol.403 , pp. 239-244
    • Pierres, A.1    Benoliel, A.M.2    Bongrand, P.3    Van Der Merwe, P.A.4
  • 36
    • 0027376261 scopus 로고
    • CD2-deficient mice generate virus-specific cytotoxic T lymphocytes upon infection with lymphocytic choriomeningitis
    • Evans CF, Rall GF, Killeen N, Littman D, Oldstone MBA. CD2-deficient mice generate virus-specific cytotoxic T lymphocytes upon infection with lymphocytic choriomeningitis. J Immunol 1993;151:6259-6264.
    • (1993) J Immunol , vol.151 , pp. 6259-6264
    • Evans, C.F.1    Rall, G.F.2    Killeen, N.3    Littman, D.4    Oldstone, M.B.A.5
  • 37
    • 0031059288 scopus 로고    scopus 로고
    • CD2 regulates positive selection and function of antigen-specific CD4-CD8+ T cells
    • Teh SJ, Killeen N, Tarakhovsky A, Littman DR, Teh HS. CD2 regulates positive selection and function of antigen-specific CD4-CD8+ T cells. Blood 1997;89:1308-1318.
    • (1997) Blood , vol.89 , pp. 1308-1318
    • Teh, S.J.1    Killeen, N.2    Tarakhovsky, A.3    Littman, D.R.4    Teh, H.S.5
  • 39
    • 0030061494 scopus 로고    scopus 로고
    • Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
    • Dustin ML, Ferguson LM, Chan PY, Springer TA, Golan DE. Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area. J Cell Biol 1996;132:465-474.
    • (1996) J Cell Biol , vol.132 , pp. 465-474
    • Dustin, M.L.1    Ferguson, L.M.2    Chan, P.Y.3    Springer, T.A.4    Golan, D.E.5
  • 40
    • 0030679644 scopus 로고    scopus 로고
    • Low affinity interaction of human or rat cell adhesion molecule CD2 with ligands aligns adhering membranes to achieve high physiological affinity
    • Dustin ML, et al. Low affinity interaction of human or rat cell adhesion molecule CD2 with ligands aligns adhering membranes to achieve high physiological affinity. J Biol Chem 1997;272:30889-30898.
    • (1997) J Biol Chem , vol.272 , pp. 30889-30898
    • Dustin, M.L.1
  • 41
    • 0030916178 scopus 로고    scopus 로고
    • Adhesive bond dynamics in contacts between T lymphocytes and glass-supported planar bilayers reconstituted with the immunoglobulin-related adhesion molecule CD58
    • Dustin ML. Adhesive bond dynamics in contacts between T lymphocytes and glass-supported planar bilayers reconstituted with the immunoglobulin-related adhesion molecule CD58. J Biol Chem 1997;272:15782-15788.
    • (1997) J Biol Chem , vol.272 , pp. 15782-15788
    • Dustin, M.L.1
  • 42
    • 0004251874 scopus 로고
    • Glycoprotein antigens of the lymphocyte surface and their purification by antibody affinity chromatography
    • Weir DM, Herzenberg LA, Blackwell C, Herzenberg LA, eds. London: Blackwell Scientific Publications
    • Williams AF, Barclay AN. Glycoprotein antigens of the lymphocyte surface and their purification by antibody affinity chromatography. In: Weir DM, Herzenberg LA, Blackwell C, Herzenberg LA, eds. Handbook of experimental immunology. London: Blackwell Scientific Publications; 1986.p.22.1-22.24.
    • (1986) Handbook of Experimental Immunology
    • Williams, A.F.1    Barclay, A.N.2
  • 43
    • 0021250906 scopus 로고
    • Cell adhesion: Competition between non-specific repulsion and specific bonding
    • Bell GI, Dembo M, Bongrand P. Cell adhesion: competition between non-specific repulsion and specific bonding. Biophys J 1984;45:1051-1064.
    • (1984) Biophys J , vol.45 , pp. 1051-1064
    • Bell, G.I.1    Dembo, M.2    Bongrand, P.3
  • 44
    • 0029140842 scopus 로고
    • Topology of the CD2-CD48 cell-adhesion molecule complex: Implications for antigen recognition by T cells
    • Van der Merwe PA, McNamee PN, Davies EA, Barclay AN, Davis SJ. Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells. Curr Biol 1995;5:74-84.
    • (1995) Curr Biol , vol.5 , pp. 74-84
    • Van Der Merwe, P.A.1    McNamee, P.N.2    Davies, E.A.3    Barclay, A.N.4    Davis, S.J.5
  • 45
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell GI. Models for the specific adhesion of cells to cells. Science 1978;200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 46
    • 0025847304 scopus 로고
    • Detachment of agglutinin-bonded red blood cells. I. Forces to rupture molecular-point attachments
    • Evans E, Berk D, Leung A. Detachment of agglutinin-bonded red blood cells. I. Forces to rupture molecular-point attachments. Biophys J 1991;59:838-848.
    • (1991) Biophys J , vol.59 , pp. 838-848
    • Evans, E.1    Berk, D.2    Leung, A.3
  • 47
    • 0029120757 scopus 로고
    • Molecular mechanisms determining the strength of receptor-mediated intermembrane adhesion
    • Leckband D, Müller W, Schmitt FJ, Ringsdorf H. Molecular mechanisms determining the strength of receptor-mediated intermembrane adhesion. Biophys J 1995;69:1162-1169.
    • (1995) Biophys J , vol.69 , pp. 1162-1169
    • Leckband, D.1    Müller, W.2    Schmitt, F.J.3    Ringsdorf, H.4
  • 48
    • 0031172162 scopus 로고    scopus 로고
    • Serial triggering of TCRs: A basis for the sensitivity and specificity of antigen recognition
    • Valitutti S, Lanzavecchia A. Serial triggering of TCRs: a basis for the sensitivity and specificity of antigen recognition. Immunol Today 1997;18:299-304.
    • (1997) Immunol Today , vol.18 , pp. 299-304
    • Valitutti, S.1    Lanzavecchia, A.2
  • 49
    • 0030042385 scopus 로고    scopus 로고
    • Inhibitory MHC class I receptors on NK cells and T cells
    • Lanier LL, Phillips JH. Inhibitory MHC class I receptors on NK cells and T cells. Immunol Today 1996;17:86-91.
    • (1996) Immunol Today , vol.17 , pp. 86-91
    • Lanier, L.L.1    Phillips, J.H.2
  • 50
    • 0030694234 scopus 로고    scopus 로고
    • The emerging role of CTLA-4 as an immune attenuator
    • Thompson CB, Allison JP. The emerging role of CTLA-4 as an immune attenuator. Immunity 1997;7:445-450.
    • (1997) Immunity , vol.7 , pp. 445-450
    • Thompson, C.B.1    Allison, J.P.2
  • 51
    • 0030014002 scopus 로고    scopus 로고
    • T-cell-receptor affinity and thymocyte positive selection
    • Alam SM, et al. T-cell-receptor affinity and thymocyte positive selection. Nature 1996;381:616-620.
    • (1996) Nature , vol.381 , pp. 616-620
    • Alam, S.M.1
  • 52
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • Lyons DS, et al. A TCR binds antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity 1996;5:53-61.
    • (1996) Immunity , vol.5 , pp. 53-61
    • Lyons, D.S.1
  • 55
    • 0023128403 scopus 로고
    • Similarities in sequences and cellular expression between rat CD2 and CD4 antigens
    • Williams AF, Barclay AN, Clark SJ, Paterson DJ, Willis AC. Similarities in sequences and cellular expression between rat CD2 and CD4 antigens. J Exp Med 1987;165:368-380.
    • (1987) J Exp Med , vol.165 , pp. 368-380
    • Williams, A.F.1    Barclay, A.N.2    Clark, S.J.3    Paterson, D.J.4    Willis, A.C.5
  • 57
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity
    • Stanley P. Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity. Mol Cell Biol 1989;9:377-383.
    • (1989) Mol Cell Biol , vol.9 , pp. 377-383
    • Stanley, P.1
  • 58
    • 0027456631 scopus 로고
    • Expression of soluble recombinant glycoproteins with predefined glycosylation: Application to the crystallization of the T-cell glycoprotein CD2
    • Davis SJ, et al. Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2. Protein Eng 1993;6:229-232.
    • (1993) Protein Eng , vol.6 , pp. 229-232
    • Davis, S.J.1
  • 59
    • 0028819608 scopus 로고
    • Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent
    • Davis SJ, et al. Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent. J Biol Chem 1995;270:369-375.
    • (1995) J Biol Chem , vol.270 , pp. 369-375
    • Davis, S.J.1
  • 60
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2
    • Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI. Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature 1992;360:232-239.
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 61
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution
    • Bodian DL, Jones EY, Harlos K, Stuart DI, Davis SJ. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure 1994;2:755-766.
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.J.5
  • 62
    • 0028054656 scopus 로고
    • Expression cloning of an equine T-lymphocyte glycoprotein CD2 cDNA. Structure-based analysis of conserved sequence elements
    • Tavernor AS, et al. Expression cloning of an equine T-lymphocyte glycoprotein CD2 cDNA. Structure-based analysis of conserved sequence elements. Eur J Biochem 1994;219:969-976.
    • (1994) Eur J Biochem , vol.219 , pp. 969-976
    • Tavernor, A.S.1
  • 63
    • 0029841147 scopus 로고    scopus 로고
    • CD2: An exception to the immunoglobulin superfamily concept?
    • Davis SJ, van der Merwe PA. CD2: an exception to the immunoglobulin superfamily concept? Science 1996;273:1241-1242.
    • (1996) Science , vol.273 , pp. 1241-1242
    • Davis, S.J.1    Van Der Merwe, P.A.2
  • 64
    • 0026540004 scopus 로고
    • N-glycosylation is required for human CD2 immunoadhesion functions
    • Recny MA, et al. N-glycosylation is required for human CD2 immunoadhesion functions. J Biol Chem 1992;267:22428-22434.
    • (1992) J Biol Chem , vol.267 , pp. 22428-22434
    • Recny, M.A.1
  • 65
    • 0029133626 scopus 로고
    • Conformation and function of the N-linked glycan in the adhesion domain of human CD2
    • Wyss DF, et al. Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Science 1995;269:1273-1278.
    • (1995) Science , vol.269 , pp. 1273-1278
    • Wyss, D.F.1
  • 66
    • 0028944878 scopus 로고
    • Conformational implications of asparagine-linked glycosylation
    • Imperiali B, Rickert KW. Conformational implications of asparagine-linked glycosylation. Proc Natl Acad Sci USA 1995;92:97-101.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 97-101
    • Imperiali, B.1    Rickert, K.W.2
  • 68
    • 0032510678 scopus 로고    scopus 로고
    • The role of charged residues mediating low affinity protein-protein recognition at the cell surface by CD2
    • Davis SJ, Davies EA, Tucknott MG, Jones EY, van der Merwe PA. The role of charged residues mediating low affinity protein-protein recognition at the cell surface by CD2. Proc Natl Acad Sci USA 1998;95:5490-5494.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5490-5494
    • Davis, S.J.1    Davies, E.A.2    Tucknott, M.G.3    Jones, E.Y.4    Van Der Merwe, P.A.5
  • 69
    • 0027197734 scopus 로고
    • Mutational analysis of the CD2/CD58 interaction: The binding site for CD58 lies on one face of the first domain of human CD2
    • Somoza C, Driscoll PC, Cyster JG, Williams AF. Mutational analysis of the CD2/CD58 interaction: the binding site for CD58 lies on one face of the first domain of human CD2. J Exp Med 1993;178:549-558.
    • (1993) J Exp Med , vol.178 , pp. 549-558
    • Somoza, C.1    Driscoll, P.C.2    Cyster, J.G.3    Williams, A.F.4
  • 70
    • 0027146691 scopus 로고
    • The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC′C″ face of the human CD2 adhesion domain
    • Arulanandam AR, et al. The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC′C″ face of the human CD2 adhesion domain. Proc Natl Acad Sci USA 1993;90: 11613-11617.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11613-11617
    • Arulanandam, A.R.1
  • 71
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J, Chothia C. The structure of protein-protein recognition sites. J Biol Chem 1990;265:16027-16030.
    • (1990) J Biol Chem , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 72
  • 74
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia C, Janin J. Principles of protein-protein recognition. Nature 1975;256:705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 76
    • 0028075859 scopus 로고
    • Interaction between human CD2 and CD58 involves the major beta sheet surface of each of their respective adhesion domains
    • Arulanandam AR, Kister A, McGregor MJ, Wyss DF, Wagner G, Reinherz EL. Interaction between human CD2 and CD58 involves the major beta sheet surface of each of their respective adhesion domains. J Exp Med 1994;180:1861-1871.
    • (1994) J Exp Med , vol.180 , pp. 1861-1871
    • Arulanandam, A.R.1    Kister, A.2    McGregor, M.J.3    Wyss, D.F.4    Wagner, G.5    Reinherz, E.L.6
  • 77
    • 0028967312 scopus 로고
    • Amino acid residues required for binding of lymphocyte function-associated antigen 3 (CD58) to its counter-receptor CD2
    • Osborn L, et al. Amino acid residues required for binding of lymphocyte function-associated antigen 3 (CD58) to its counter-receptor CD2. J Exp Med 1995;181:429-434.
    • (1995) J Exp Med , vol.181 , pp. 429-434
    • Osborn, L.1
  • 78
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 1996;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.C.6
  • 79
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in the T cell receptor recognition of a self peptide-MHC antigen
    • Garcia KC, et al. Structural basis of plasticity in the T cell receptor recognition of a self peptide-MHC antigen. Science 1998;279:1166-1172.
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1
  • 80
    • 0027730137 scopus 로고
    • Measuring very low affinity interactions between immunoglobulin superfamily cell-adhesion molecules
    • Van der Merwe PA, Brown MH, Davis SJ, Barclay AN. Measuring very low affinity interactions between immunoglobulin superfamily cell-adhesion molecules. Biochem Soc Trans 1993;21:340S.
    • (1993) Biochem Soc Trans , vol.21
    • Van Der Merwe, P.A.1    Brown, M.H.2    Davis, S.J.3    Barclay, A.N.4
  • 81
    • 0030246987 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin
    • Shapiro L, Doyle JP, Hensley P, Colman DR, Hendrickson WA. Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin. Neuron 1996;17:435-449.
    • (1996) Neuron , vol.17 , pp. 435-449
    • Shapiro, L.1    Doyle, J.P.2    Hensley, P.3    Colman, D.R.4    Hendrickson, W.A.5
  • 82
    • 0028924936 scopus 로고
    • Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 Å resolution
    • Jones EY, et al. Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 Å resolution. Nature 1995;373:539-544.
    • (1995) Nature , vol.373 , pp. 539-544
    • Jones, E.Y.1
  • 83
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson R, Michaelsson A, Mattsson L. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J Immunol Methods 1991;145:229-240.
    • (1991) J Immunol Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 84
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. Molscript: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallography 1991;24:946-950.
    • (1991) J Appl Crystallography , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 87
    • 0027383871 scopus 로고
    • Cloning and characterization of the 2B4 gene encoding a molecule associated with non-MHC-restricted killing mediated by activated natural killer cells and T cells
    • Mathew PA, et al. Cloning and characterization of the 2B4 gene encoding a molecule associated with non-MHC-restricted killing mediated by activated natural killer cells and T cells. J Immunol 1993;151:5328-5337.
    • (1993) J Immunol , vol.151 , pp. 5328-5337
    • Mathew, P.A.1
  • 88
    • 0026782892 scopus 로고
    • Isolation and characterization of cDNA clones for mouse Ly-9
    • Sandrin MS, et al. Isolation and characterization of cDNA clones for mouse Ly-9. J Immunol 1992;149:1636-1641.
    • (1992) J Immunol , vol.149 , pp. 1636-1641
    • Sandrin, M.S.1
  • 89
    • 0026319199 scopus 로고
    • Protein folding and association; insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp K, Honig B. Protein folding and association; insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 90
    • 0029918134 scopus 로고    scopus 로고
    • Localization of the putative sialic acid binding site on the immunoglobulin superfamily cell surface molecule CD22
    • Van der Merwe PA, Crocker P, Vincent M, Barclay AN, Kelm S. Localization of the putative sialic acid binding site on the immunoglobulin superfamily cell surface molecule CD22. J Biol Chem 1996;271:9273-9280.
    • (1996) J Biol Chem , vol.271 , pp. 9273-9280
    • Van Der Merwe, P.A.1    Crocker, P.2    Vincent, M.3    Barclay, A.N.4    Kelm, S.5
  • 91
    • 0029931973 scopus 로고    scopus 로고
    • Characterization of the sialic acid-binding site in sialoadhesin by site-directed mutagenesis
    • Vinson M, van der Merwe PA, Kelm S, May A, Jones EY, Crocker PR. Characterization of the sialic acid-binding site in sialoadhesin by site-directed mutagenesis. J Biol Chem 1996;271:9267-9272.
    • (1996) J Biol Chem , vol.271 , pp. 9267-9272
    • Vinson, M.1    Van Der Merwe, P.A.2    Kelm, S.3    May, A.4    Jones, E.Y.5    Crocker, P.R.6
  • 92
    • 0023626760 scopus 로고
    • Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)
    • Peterson A, Seed B. Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2). Nature 1987;329:842-846.
    • (1987) Nature , vol.329 , pp. 842-846
    • Peterson, A.1    Seed, B.2
  • 93
    • 0029133256 scopus 로고
    • Both extracellular immunoglobulin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28
    • Peach RJ, et al. Both extracellular immunoglobulin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28. J Biol Chem 1995;270:21181-21187.
    • (1995) J Biol Chem , vol.270 , pp. 21181-21187
    • Peach, R.J.1
  • 94
    • 0031180381 scopus 로고    scopus 로고
    • Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28
    • Metzler WJ, et al. Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28. Nat Struct Biol 1997;4:527-531.
    • (1997) Nat Struct Biol , vol.4 , pp. 527-531
    • Metzler, W.J.1
  • 95
    • 0030983812 scopus 로고    scopus 로고
    • CD6-ligand interactions: A paradigm for SRCR domain function?
    • Aruffo A, et al. CD6-ligand interactions: a paradigm for SRCR domain function? Immunol Today 1997;18:498-504.
    • (1997) Immunol Today , vol.18 , pp. 498-504
    • Aruffo, A.1
  • 96
    • 0030786994 scopus 로고    scopus 로고
    • Characterization of the low affinity interaction between rat cell adhesion molecules CD2 and CD48 by analytical ultracentrifugation
    • Silkowski H, Davis SJ, Barclay AN, Rowe AJ, Harding SE, Byron O. Characterization of the low affinity interaction between rat cell adhesion molecules CD2 and CD48 by analytical ultracentrifugation. Eur Biophys J 1997;25:455-462.
    • (1997) Eur Biophys J , vol.25 , pp. 455-462
    • Silkowski, H.1    Davis, S.J.2    Barclay, A.N.3    Rowe, A.J.4    Harding, S.E.5    Byron, O.6
  • 97
    • 0028589333 scopus 로고
    • Kinetics of T-cell receptor binding to peptide/I-Ek complexes: Correlation of the dissociation rate with T-cell responsiveness
    • Matsui K, Boniface JJ, Steffner P, Reay PA, Davis MM. Kinetics of T-cell receptor binding to peptide/I-Ek complexes: correlation of the dissociation rate with T-cell responsiveness. Proc Natl Acad Sci USA 1994;91: 12862-12866.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12862-12866
    • Matsui, K.1    Boniface, J.J.2    Steffner, P.3    Reay, P.A.4    Davis, M.M.5
  • 98
    • 0029807351 scopus 로고    scopus 로고
    • CD8 enhances formation of stable T-cell receptor/MHC class I molecule complexes
    • Garcia KC, et al. CD8 enhances formation of stable T-cell receptor/MHC class I molecule complexes. Nature 1996;384:577-581.
    • (1996) Nature , vol.384 , pp. 577-581
    • Garcia, K.C.1
  • 99
    • 0027169408 scopus 로고
    • Mouse CD4 binds MHC class II with extremely low affinity
    • Weber S, Karjalainen K. Mouse CD4 binds MHC class II with extremely low affinity. Int Immunol 1993;5:695-698.
    • (1993) Int Immunol , vol.5 , pp. 695-698
    • Weber, S.1    Karjalainen, K.2
  • 100
    • 0029901736 scopus 로고    scopus 로고
    • Direct binding of a soluble natural killer cell inhibitory receptor to a soluble human leukocyte antigen-Cw4 class I major histocompatibility complex molecule
    • Fan QR, Garbozi DN, Winter CC, Wagtmann N, Long EO, Wiley DC. Direct binding of a soluble natural killer cell inhibitory receptor to a soluble human leukocyte antigen-Cw4 class I major histocompatibility complex molecule. Proc Natl Acad Sci USA 1996;93:7178-7183.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7178-7183
    • Fan, Q.R.1    Garbozi, D.N.2    Winter, C.C.3    Wagtmann, N.4    Long, E.O.5    Wiley, D.C.6
  • 101
    • 0027364840 scopus 로고
    • Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated cells
    • Lollo BA, Chan KWH, Hanson EM, Moy VT, Brian AA. Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated cells. J Biol Chem 1993;268:21693-21700.
    • (1993) J Biol Chem , vol.268 , pp. 21693-21700
    • Lollo, B.A.1    Chan, K.W.H.2    Hanson, E.M.3    Moy, V.T.4    Brian, A.A.5
  • 102
    • 0028962757 scopus 로고
    • Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22 - Evidence for a minimal structural recognition motif and the potential importance of multisite binding
    • Powell LD, Jain RK, Matta KL, Sabesan S, Varki A. Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22 - evidence for a minimal structural recognition motif and the potential importance of multisite binding. J Biol Chem 1995;270:7523-7532.
    • (1995) J Biol Chem , vol.270 , pp. 7523-7532
    • Powell, L.D.1    Jain, R.K.2    Matta, K.L.3    Sabesan, S.4    Varki, A.5


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