메뉴 건너뛰기




Volumn 387, Issue 6631, 1997, Pages 426-430

Atomic structure of the ectodomain from HIV-1 gp41

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 41;

EID: 0030962291     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/387426a0     Document Type: Article
Times cited : (1494)

References (35)
  • 1
    • 0021997051 scopus 로고
    • Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III
    • Allan, J. S. et al. Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III. Science 228, 1091-1094 (1985).
    • (1985) Science , vol.228 , pp. 1091-1094
    • Allan, J.S.1
  • 2
    • 0022352075 scopus 로고
    • Characterization of gp41 as the transmembrane protein coded by the HTLV-III/ LAV envelope gene
    • Veronese, F. D. et al. Characterization of gp41 as the transmembrane protein coded by the HTLV-III/ LAV envelope gene. Science 229, 1402-1405 (1985).
    • (1985) Science , vol.229 , pp. 1402-1405
    • Veronese, F.D.1
  • 3
    • 0029802605 scopus 로고    scopus 로고
    • Chemokines and HIV-1 second receptors: Confluence of two fields generates optimism in AIDS research
    • D'Souza, M. P. & Harden, V. A. Chemokines and HIV-1 second receptors: confluence of two fields generates optimism in AIDS research. Nat. Med. 2, 1293-1300 (1996).
    • (1996) Nat. Med. , vol.2 , pp. 1293-1300
    • D'Souza, M.P.1    Harden, V.A.2
  • 4
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow, S. C., Lu, M. & Kim, P. S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry 34, 14955-14962 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 5
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., Blacklow, S. C. & Kim, P. S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct. Biol. 2, 1075-1082 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 6
    • 25944471518 scopus 로고    scopus 로고
    • Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 Gp41 ectodomain expressed in E. coli
    • in the press
    • Weissenhorn, W. et al. Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 Gp41 ectodomain expressed in E. coli. Proc. Natl Acad. Sci. USA (in the press).
    • Proc. Natl Acad. Sci. USA
    • Weissenhorn, W.1
  • 7
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J. & Wiley, D. C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43 (1994).
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 8
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 Å resolution
    • Fass, D., Harrison, S. C. & Kim, P. S. Retrovirus envelope domain at 1.7 Å resolution. Nature Struct. Biol. 3, 465-469 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 9
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P. B., Kim, P. S. & Alber, T. Crystal structure of an isoleucine-zipper trimer. Nature 371, 80-83 (1994).
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 10
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P., Pringle, C. R. & Easton, A. J. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71, 3075-3080 (1980).
    • (1980) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 12
    • 0029878665 scopus 로고    scopus 로고
    • The ectodomain of HFV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide
    • Weissenhorn, W. et al. The ectodomain of HFV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO J. 15, 1507-1514 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1507-1514
    • Weissenhorn, W.1
  • 13
    • 0000747247 scopus 로고
    • The Fourier transform of a coiled-coil
    • Crick, F. H. C. The Fourier transform of a coiled-coil. Acta Crystallogr. 6, 685 (1953).
    • (1953) Acta Crystallogr. , vol.6 , pp. 685
    • Crick, F.H.C.1
  • 14
    • 0020035202 scopus 로고
    • Changes in the conformation of influenza virus haemagglutinin at the pH optimum of virus-mediated membrane fusion
    • Skehel, J. J. et al. Changes in the conformation of influenza virus haemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc. Natl Acad. Sci. USA 79, 968-972 (1982).
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 968-972
    • Skehel, J.J.1
  • 15
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M. & Kim, P. S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832 (1993).
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 16
    • 0023716861 scopus 로고
    • Studies on the structure of the influenza virus haemagglutinin at the pH of membrane fusion
    • Ruigrok, R. W. et al. Studies on the structure of the influenza virus haemagglutinin at the pH of membrane fusion. J. Gen. Virol. 69, 2785-2795 (1988).
    • (1988) J. Gen. Virol. , vol.69 , pp. 2785-2795
    • Ruigrok, R.W.1
  • 17
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    • Wharton, S. A. et al. Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO J. 14, 240-246 (1995).
    • (1995) EMBO J. , vol.14 , pp. 240-246
    • Wharton, S.A.1
  • 18
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by souble CD4
    • Moore, J. P., McKeating, J. A., Weiss, R. A. & Sattentau, Q. J. Dissociation of gp120 from HIV-1 virions induced by souble CD4. Science 250, 1139-1142 (1990).
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 19
    • 0026011315 scopus 로고
    • Binding of soluble CD4 proteins to human immunodeficiency virus type1 and infected cells induces release of envelope glycoprotein gp120
    • Hart, T. K. et al. binding of soluble CD4 proteins to human immunodeficiency virus type1 and infected cells induces release of envelope glycoprotein gp120. Proc. Natl Acad. Sci. USA 88, 2189-2193 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2189-2193
    • Hart, T.K.1
  • 20
    • 0025152268 scopus 로고
    • Morphometic analysis of recombinant soluble CD4-mediated release of the envelope glycoprotein gp120 from HIV-1
    • Kirsh, R. et al. Morphometic analysis of recombinant soluble CD4-mediated release of the envelope glycoprotein gp120 from HIV-1. AIDS Res. Hum. Retroviruses 6, 1209-1212 (1990).
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 1209-1212
    • Kirsh, R.1
  • 21
    • 0029558245 scopus 로고
    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation
    • Chen, J. et al. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc. Natl Acad. Sci. USA 92, 12205-12209 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12205-12209
    • Chen, J.1
  • 22
    • 0026465468 scopus 로고
    • A synthetic inhibitor of human immunodeficiency virus replciation: Correlation between solution structure and viral inhibition
    • Wild, C. T., Oas, T., McDanal, C. B., Bolognesi, D. & Matthews, T. A synthetic inhibitor of human immunodeficiency virus replciation: Correlation between solution structure and viral inhibition. Proc. Natl Acad. Sci. USA 89, 10537-10541 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.T.1    Oas, T.2    McDanal, C.B.3    Bolognesi, D.4    Matthews, T.5
  • 23
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 and gp41 are potent inhibitors of virus infection
    • Wild, C. T., Shugars, D. C., Greenwell, T. K., McDanal, C. B. & Matthews, T. J. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 and gp41 are potent inhibitors of virus infection. Proc. Natl Acad. Sci. USA 91, 9770-9774 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 24
    • 0029072191 scopus 로고
    • A molecular clasp in th ehuman immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: Implication for viral fusion
    • Chen, C. H., Matthews, T. J., McDanal, C. B., Bolognesi, D. P. & Greenberg, M. L. A molecular clasp in th ehuman immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J. Virol. 69, 3771-3777 (1995).
    • (1995) J. Virol. , vol.69 , pp. 3771-3777
    • Chen, C.H.1    Matthews, T.J.2    McDanal, C.B.3    Bolognesi, D.P.4    Greenberg, M.L.5
  • 25
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay, J. W., Roberts, S. J., Brody, B. & Hunter, E. Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66, 4748-4756 (1992).
    • (1992) J. Virol. , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 26
    • 0029556492 scopus 로고    scopus 로고
    • Membrane Fusion by Influenza Hemagglutinin
    • Skehel, J. J. et al. Membrane Fusion by Influenza Hemagglutinin. Cold Spring Harb. Symp. Quant. Biol. 60, 573-580 (1996).
    • (1996) Cold Spring Harb. Symp. Quant. Biol. , vol.60 , pp. 573-580
    • Skehel, J.J.1
  • 27
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C. & Harrison, S. C. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375, 291-298 (1995).
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 29
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli, T., Pelletier, S. L., Henis, Y. I. & White, J. M. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133, 559-569 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 30
    • 0030965051 scopus 로고    scopus 로고
    • Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy
    • in the press
    • Kanaseki, T., Kawasaki, K., Murata, M., Ikeuchi, Y. & Ohnishi, S.-I. Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy. J. Cell Biol. (in the press).
    • J. Cell Biol.
    • Kanaseki, T.1    Kawasaki, K.2    Murata, M.3    Ikeuchi, Y.4    Ohnishi, S.-I.5
  • 31
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M. & Kim, P. S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273 (1997).
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 32
    • 0028103275 scopus 로고
    • CCP4 the CCP4 Suite: Programs for Protein Crystallography
    • CCP4 The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D 50, 760-776 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-776
  • 35
    • 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, 924-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 924-950
    • Kraulis, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.