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Volumn 335, Issue 2, 2005, Pages 276-285

Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein

Author keywords

Asparagine zipper; Class I fusion protein; Coiled coil; Heptad repeat; Membrane fusion; SARS; Spike protein; Structure

Indexed keywords

ASPARAGINE; CHLORIDE ION; GLUTAMINE; VIRUS FUSION PROTEIN; VIRUS GLYCOPROTEIN;

EID: 17444401009     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2005.02.022     Document Type: Article
Times cited : (90)

References (25)
  • 1
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • D.L. Akey, V.N. Malashkevich, and P.S. Kim Buried polar residues in coiled-coil interfaces Biochemistry 40 21 2001 6352 6360
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 2
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • K.A. Baker, R.E. Dutch, R.A. Lamb, and T.S. Jardetzky Structural basis for paramyxovirus-mediated membrane fusion Mol. Cell 3 3 1999 309 319
    • (1999) Mol. Cell , vol.3 , Issue.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 3
    • 0042208243 scopus 로고    scopus 로고
    • The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex
    • B.J. Bosch, R. Van Der Zee, C.A. De Haan, and P.J. Rottier The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex J. Virol. 77 16 2003 8801 8811
    • (2003) J. Virol. , vol.77 , Issue.16 , pp. 8801-8811
    • Bosch, B.J.1    Van Der Zee, R.2    De Haan, C.A.3    Rottier, P.J.4
  • 5
    • 0033529752 scopus 로고    scopus 로고
    • N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA2 subunit to form an N cap that terminates the triple-stranded coiled coil
    • J. Chen, J.J. Skehel, and D.C. Wiley N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA2 subunit to form an N cap that terminates the triple-stranded coiled coil Proc. Natl. Acad. Sci. U. S. A. 96 1999 8967 8972
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 6
    • 0000747247 scopus 로고
    • The Fourier transform of a coiled-coil
    • F.H.C. Crick The Fourier transform of a coiled-coil Acta Crystallogr. 6 1953 685 689
    • (1953) Acta Crystallogr. , vol.6 , pp. 685-689
    • Crick, F.H.C.1
  • 8
    • 0025103827 scopus 로고
    • Assembly of coronavirus spike protein into trimers and its role in epitope expression
    • B. Delmas, and H. Laude Assembly of coronavirus spike protein into trimers and its role in epitope expression J. Virol. 64 11 1990 5367 5375
    • (1990) J. Virol. , vol.64 , Issue.11 , pp. 5367-5375
    • Delmas, B.1    Laude, H.2
  • 9
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 angstrom resolution
    • D. Fass, S.C. Harrison, and P.S. Kim Retrovirus envelope domain at 1.7 angstrom resolution Nat. Struct. Biol. 3 5 1996 465 469
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.5 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 11
    • 0032827589 scopus 로고    scopus 로고
    • Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion
    • Z. Luo, A.M. Matthews, and S.R. Weiss Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion J. Virol. 73 10 1999 8152 8159
    • (1999) J. Virol. , vol.73 , Issue.10 , pp. 8152-8159
    • Luo, Z.1    Matthews, A.M.2    Weiss, S.R.3
  • 13
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • L. Pauling, R.B. Corey, and H.R. Branson The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain Proc. Natl. Acad. Sci. U. S. A. 37 4 1951 205 211
    • (1951) Proc. Natl. Acad. Sci. U. S. A. , vol.37 , Issue.4 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 14
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • L.G. Presta, and G.D. Rose Helix signals in proteins Science 240 1988 1632 1641
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 15
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a helices
    • J.S. Richardson, and D.C. Richardson Amino acid preferences for specific locations at the ends of a helices Science 240 1988 1648 1652
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 16
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • J.J. Skehel, and D.C. Wiley Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin Annu. Rev. Biochem. 69 2000 531 569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 17
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • A.E. Smith, and A. Helenius How viruses enter animal cells Science 304 2004 237 242
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 18
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • S.V. Strelkov, and P. Burkhard Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation J. Struct. Biol. 137 1-2 2002 54 64
    • (2002) J. Struct. Biol. , vol.137 , Issue.1-2 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 19
    • 11144237311 scopus 로고    scopus 로고
    • Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein
    • V.M. Supekar, C. Bruckmann, P. Ingallinella, E. Bianchi, A. Pessi, and A. Carfi Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein Proc. Natl. Acad. Sci. U. S. A. 101 52 2004 17958 17963
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.52 , pp. 17958-17963
    • Supekar, V.M.1    Bruckmann, C.2    Ingallinella, P.3    Bianchi, E.4    Pessi, A.5    Carfi, A.6
  • 20
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 21
    • 2442698802 scopus 로고    scopus 로고
    • Structural characterization of the SARS-coronavirus spike S fusion protein core
    • B. Tripet, M.W. Howard, M. Jobling, R.K. Holmes, K.V. Holmes, and R.S. Hodges Structural characterization of the SARS-coronavirus spike S fusion protein core J. Biol. Chem. 279 20 2004 20836 20849
    • (2004) J. Biol. Chem. , vol.279 , Issue.20 , pp. 20836-20849
    • Tripet, B.1    Howard, M.W.2    Jobling, M.3    Holmes, R.K.4    Holmes, K.V.5    Hodges, R.S.6
  • 22
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • W. Weissenhorn, A. Carfi, K.H. Lee, J.J. Skehel, and D.C. Wiley Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain Mol. Cell 2 5 1998 605 616
    • (1998) Mol. Cell , vol.2 , Issue.5 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 23
    • 8344260757 scopus 로고    scopus 로고
    • Characterization of the heptad repeat regions, HR1 and HR2, and design of a fusion core structure model of the spike protein from severe acute respiratory syndrome (SARS) coronavirus
    • Y. Xu, J. Zhu, Y. Liu, Z. Lou, F. Yuan, Y. Liu, D.K. Cole, L. Ni, N. Su, L. Qin, X. Li, Z. Bai, J.I. Bell, H. Pang, P. Tien, G.F. Gao, and Z. Rao Characterization of the heptad repeat regions, HR1 and HR2, and design of a fusion core structure model of the spike protein from severe acute respiratory syndrome (SARS) coronavirus Biochemistry 43 44 2004 14064 14071
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14064-14071
    • Xu, Y.1    Zhu, J.2    Liu, Y.3    Lou, Z.4    Yuan, F.5    Liu, Y.6    Cole, D.K.7    Ni, L.8    Su, N.9    Qin, L.10    Li, X.11    Bai, Z.12    Bell, J.I.13    Pang, H.14    Tien, P.15    Gao, G.F.16    Rao, Z.17
  • 24
    • 10344234242 scopus 로고    scopus 로고
    • Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core
    • Y. Xu, Z. Lou, Y. Liu, H. Pang, P. Tien, G.F. Gao, and Z. Rao Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core J. Biol. Chem. 279 47 2004 49414 49419
    • (2004) J. Biol. Chem. , vol.279 , Issue.47 , pp. 49414-49419
    • Xu, Y.1    Lou, Z.2    Liu, Y.3    Pang, H.4    Tien, P.5    Gao, G.F.6    Rao, Z.7
  • 25
    • 3142663245 scopus 로고    scopus 로고
    • Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core
    • Y. Xu, Y. Liu, Z. Lou, L. Qin, X. Li, Z. Bai, H. Pang, P. Tien, G.F. Gao, and Z. Rao Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core J. Biol. Chem. 279 29 2004 30514 30522
    • (2004) J. Biol. Chem. , vol.279 , Issue.29 , pp. 30514-30522
    • Xu, Y.1    Liu, Y.2    Lou, Z.3    Qin, L.4    Li, X.5    Bai, Z.6    Pang, H.7    Tien, P.8    Gao, G.F.9    Rao, Z.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.