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Volumn 387, Issue 6630, 1997, Pages 312-315

Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface

Author keywords

[No Author keywords available]

Indexed keywords

CD11 ANTIGEN; CD18 ANTIGEN; INTEGRIN; INTERCELLULAR ADHESION MOLECULE 2; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; VASCULAR CELL ADHESION MOLECULE 1;

EID: 0030916713     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/387312a0     Document Type: Article
Times cited : (104)

References (31)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25 (1992).
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 2
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multi-step paradigm
    • Springer, T. A. Traffic signals for lymphocyte recirculation and leukocyte emigration: The multi-step paradigm. Cell 76, 301-314 (1994).
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 3
    • 0028986196 scopus 로고
    • Crystal structure of the a domain from the α-subunit of integrin CR3 (CD11b/CD18)
    • Lee, J.-O., Rieu, P., Arnaout, M. A. & Liddington, R. Crystal structure of the A domain from the α-subunit of integrin CR3 (CD11b/CD18). Cell 80, 631-638 (1995).
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 5
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D. J., Aukhil, I. & Erickson, H. P. 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155-164 (1996).
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 6
    • 0028924936 scopus 로고
    • Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 Å resolution
    • Jones, E. Y. et al. Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 Å resolution. Nature 373, 539-544 (1995).
    • (1995) Nature , vol.373 , pp. 539-544
    • Jones, E.Y.1
  • 7
    • 0029046132 scopus 로고
    • The crystal structure of an N-terminal two domain fragment of VCAM-1: A cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1/α4 integrin
    • Wang, J.-h. et al. The crystal structure of an N-terminal two domain fragment of VCAM-1: A cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1/α4 integrin. Proc. Natl Acad. Sci. USA 92, 5714-5718 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5714-5718
    • Wang, J.-H.1
  • 8
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycopoteins with minimal carbohydrate heterogeneity
    • Stanley, P. Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycopoteins with minimal carbohydrate heterogeneity. Mol. Cell. Biol. 9, 377-383 (1989).
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 377-383
    • Stanley, P.1
  • 9
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
    • Staunton, D. E., Dustin, M. L., Erickson, H. P. & Springer, T. A. The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus. Cell 61, 243-254 (1990).
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 10
    • 0028924958 scopus 로고
    • Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1
    • Holness, C. L. et al. Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1. J. Biol. Chem. 270, 877-884 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 877-884
    • Holness, C.L.1
  • 11
    • 0029845205 scopus 로고    scopus 로고
    • Localization of the binding site on intercellular adhesion molecule-3 (ICAM-3) for lymphocyte function-associated antigen-1 (LFA-1)
    • Klickstein, L. B., York, M. B., de Fougerolles, A. R. & Springer, T. A. Localization of the binding site on intercellular adhesion molecule-3 (ICAM-3) for lymphocyte function-associated antigen-1 (LFA-1). J. Biol. Chem. 271, 23920-23927 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 23920-23927
    • Klickstein, L.B.1    York, M.B.2    De Fougerolles, A.R.3    Springer, T.A.4
  • 12
    • 0027995549 scopus 로고
    • LFA-1 binding site in ICAM-3 contains a conserved motif and non-contiguous amino acids
    • Sadhu, C. et al. LFA-1 binding site in ICAM-3 contains a conserved motif and non-contiguous amino acids. Cell Adhes. Commun. 2, 429-440 (1994).
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 429-440
    • Sadhu, C.1
  • 13
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz, Y. & Chothia, C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238, 528-539 (1994).
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 14
    • 0002738505 scopus 로고
    • A year in the life of the immunoglobulin superfamily
    • Williams, A. F. A year in the life of the immunoglobulin superfamily. Immunol. Today 8, 298-303 (1987).
    • (1987) Immunol. Today , vol.8 , pp. 298-303
    • Williams, A.F.1
  • 15
    • 0030042397 scopus 로고    scopus 로고
    • Structure of a functional fragment of VCAM-1 refined at 1.9 Å resolution
    • Wang, J.-h. et al. Structure of a functional fragment of VCAM-1 refined at 1.9 Å resolution. Acta Crystallogr. 52, 369-379 (1996).
    • (1996) Acta Crystallogr. , vol.52 , pp. 369-379
    • Wang, J.-H.1
  • 16
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution
    • Bodian, D. L., Jones, E. Y., Harlos, K., Stuart, D. I. & Davis, S. J. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure 2, 755-766 (1995).
    • (1995) 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
  • 17
    • 0029588555 scopus 로고
    • Complex salt bridges in proteins: Statistical analysis of structure and function
    • Musafia, B., Buchner, V. & Arad, D. Complex salt bridges in proteins: Statistical analysis of structure and function. J. Mol. Biol. 254, 761-770 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 761-770
    • Musafia, B.1    Buchner, V.2    Arad, D.3
  • 18
    • 0029059578 scopus 로고
    • A binding interface on the I domain of lymphocyte function associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1)
    • Huang, C. & Springer, T. A. A binding interface on the I domain of lymphocyte function associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1). J. Biol. Chem. 270, 19008-19016 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 19008-19016
    • Huang, C.1    Springer, T.A.2
  • 19
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain
    • Springer, T. A. Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. Proc. Natl Acad. Sci. USA 94, 65-72 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 20
    • 0024542689 scopus 로고
    • The major human rhinovirus receptor is ICAM-1
    • Greve, J. M. et al. The major human rhinovirus receptor is ICAM-1. Cell 56, 839-847 (1989).
    • (1989) Cell , vol.56 , pp. 839-847
    • Greve, J.M.1
  • 21
    • 0024521781 scopus 로고
    • A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses
    • Staunton, D. E. et al. A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses. Cell 56, 849-853 (1989).
    • (1989) Cell , vol.56 , pp. 849-853
    • Staunton, D.E.1
  • 22
    • 0024416636 scopus 로고
    • Intercellular adhesion molecule-1 is an endothelial cell adhesion receptor for Plasmodium falciparum
    • Berendt, A. R., Simmons, D. L., Tansey, J., Newbold, C. I. & Marsh, K. Intercellular adhesion molecule-1 is an endothelial cell adhesion receptor for Plasmodium falciparum. Nature 341, 57-59 (1989).
    • (1989) Nature , vol.341 , pp. 57-59
    • Berendt, A.R.1    Simmons, D.L.2    Tansey, J.3    Newbold, C.I.4    Marsh, K.5
  • 23
    • 0025887767 scopus 로고
    • Identification of monoclonal antibody epitopes and critical residues for rhinovirus binding in domain 1 of intercellular adhesion molecule 1
    • McClelland, A. et al. Identification of monoclonal antibody epitopes and critical residues for rhinovirus binding in domain 1 of intercellular adhesion molecule 1. Proc. Natl Acad. Sci. USA 88, 7993-7997 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7993-7997
    • McClelland, A.1
  • 24
    • 0025789993 scopus 로고
    • Human-murine chimeras of ICAM-1 identify amino acid residues critical for rhinovirus and antibody binding
    • Register, R. B., Uncapher, C. R., Naylor, A. M., Lineberger, D. W. & Colonno, R. J. Human-murine chimeras of ICAM-1 identify amino acid residues critical for rhinovirus and antibody binding. J. Virol. 65, 6589-6596 (1991).
    • (1991) J. Virol. , vol.65 , pp. 6589-6596
    • Register, R.B.1    Uncapher, C.R.2    Naylor, A.M.3    Lineberger, D.W.4    Colonno, R.J.5
  • 25
    • 0026580223 scopus 로고
    • Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus
    • Ockenhouse, C. F., Betageri, R., Springer, T. A. & Staunton, D. E. Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus. Cell 68, 63-69 (1992).
    • (1992) Cell , vol.68 , pp. 63-69
    • Ockenhouse, C.F.1    Betageri, R.2    Springer, T.A.3    Staunton, D.E.4
  • 26
    • 0026542081 scopus 로고
    • The binding site on ICAM-1 for plasmodium falciparum-infected erythorcytes overlaps, but is distinct from, the LFA-1-binding site
    • Berendt, A. R. et al. The binding site on ICAM-1 for plasmodium falciparum-infected erythorcytes overlaps, but is distinct from, the LFA-1-binding site. Cell 68, 71-81 (1992).
    • (1992) Cell , vol.68 , pp. 71-81
    • Berendt, A.R.1
  • 27
    • 0024592732 scopus 로고
    • Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1
    • Staunton, D. E., Dustin, M. L. & Springer, T. A. Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1. Nature 339, 61-64 (1989).
    • (1989) Nature , vol.339 , pp. 61-64
    • Staunton, D.E.1    Dustin, M.L.2    Springer, T.A.3
  • 28
    • 0029063466 scopus 로고
    • Kinetics and thermodynamics of virus binding to receptor: Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance
    • Casasnovas, J. M. & Springer, T. A. Kinetics and thermodynamics of virus binding to receptor: Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance. J. Biol. Chem. 270, 13216-13224 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 13216-13224
    • Casasnovas, J.M.1    Springer, T.A.2
  • 29
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M. Ribbon models of macromolecules. J. Mol. Graph. 5, 103-106 (1987).
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.1
  • 30
    • 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
  • 31
    • 1842383153 scopus 로고
    • Thesis, Univ. London
    • Sali, A. Thesis, Univ. London, 1991.
    • (1991)
    • Sali, A.1


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