메뉴 건너뛰기




Volumn 233, Issue 1, 1997, Pages 163-173

The influenza A virus M2 channel: A molecular modeling and simulation study

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; MEMBRANE PROTEIN; VIRUS PROTEIN;

EID: 0030803839     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8578     Document Type: Article
Times cited : (135)

References (65)
  • 3
    • 0030579817 scopus 로고    scopus 로고
    • Simulation of voltage-dependent interactions of α-helical peptides with lipid bilayers
    • Biggin P. C., Sansom M. S. P. Simulation of voltage-dependent interactions of α-helical peptides with lipid bilayers. Biophys. Chem. 60:1996;99-110.
    • (1996) Biophys. Chem. , vol.60 , pp. 99-110
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 4
    • 0029863372 scopus 로고    scopus 로고
    • Molecular dynamics simulations of water within models of transbilayer pores
    • Breed J., Sankararamakrishnan R., Kerr I. D., Sansom M. S. P. Molecular dynamics simulations of water within models of transbilayer pores. Biophys. J. 70:1996;1643-1661.
    • (1996) Biophys. J. , vol.70 , pp. 1643-1661
    • Breed, J.1    Sankararamakrishnan, R.2    Kerr, I.D.3    Sansom, M.S.P.4
  • 7
    • 0029816765 scopus 로고    scopus 로고
    • Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells
    • Chizhmakov I. V., Geraghty F. M., Ogden D. C., Hayhurst A., Antoniou M., Hay A. J. Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells. J. Physiol. 494:1996;329-336.
    • (1996) J. Physiol. , vol.494 , pp. 329-336
    • Chizhmakov, I.V.1    Geraghty, F.M.2    Ogden, D.C.3    Hayhurst, A.4    Antoniou, M.5    Hay, A.J.6
  • 9
    • 0026772384 scopus 로고
    • Evidence that the amantadine-induced, M2-mediated conversion of influenza-A virus haemagglutinin to the low pH conformation occurs in an acidictrans
    • Ciampor F., Bayley P. M., Nermut M. V., Hirst E. M. A., Sugrue R. J., Hay A. J. Evidence that the amantadine-induced, M2-mediated conversion of influenza-A virus haemagglutinin to the low pH conformation occurs in an acidictrans. Virology. 188:1992;14-24.
    • (1992) Virology , vol.188 , pp. 14-24
    • Ciampor, F.1    Bayley, P.M.2    Nermut, M.V.3    Hirst, E.M.A.4    Sugrue, R.J.5    Hay, A.J.6
  • 10
    • 0030183308 scopus 로고    scopus 로고
    • Visualizing proton conductance in the gramicidin channel
    • Deamer D. W. Visualizing proton conductance in the gramicidin channel. Biophys. J. 71:1996;5.
    • (1996) Biophys. J. , vol.71 , pp. 5
    • Deamer, D.W.1
  • 11
    • 0030950444 scopus 로고    scopus 로고
    • Deuterium isotope effects on permeation and gating of proton channels in rat alveolar epithelium
    • DeCoursey T. E., Cherny V. V. Deuterium isotope effects on permeation and gating of proton channels in rat alveolar epithelium. J. Gen. Physiol. 109:1997;415-434.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 415-434
    • Decoursey, T.E.1    Cherny, V.V.2
  • 12
    • 0026785994 scopus 로고
    • The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
    • Duff K. C., Ashley R. H. The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers. Virology. 190:1992;485-489.
    • (1992) Virology , vol.190 , pp. 485-489
    • Duff, K.C.1    Ashley, R.H.2
  • 13
    • 0026745087 scopus 로고
    • The secondary structure of influenza A M2 transmembrane domain
    • Duff K. C., Kelly S. M., Price N. C., Bradshaw J. P. The secondary structure of influenza A M2 transmembrane domain. FEBS Lett. 311:1992;256-258.
    • (1992) FEBS Lett. , vol.311 , pp. 256-258
    • Duff, K.C.1    Kelly, S.M.2    Price, N.C.3    Bradshaw, J.P.4
  • 14
    • 0024288356 scopus 로고
    • The structure of a membrane-spanning polypeptide studied by molecular dynamics
    • Edholm O., Jähnig F. The structure of a membrane-spanning polypeptide studied by molecular dynamics. Biophys. Chem. 30:1988;279-292.
    • (1988) Biophys. Chem. , vol.30 , pp. 279-292
    • Edholm, O.1    Jähnig, F.2
  • 15
    • 0029794387 scopus 로고    scopus 로고
    • The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels
    • Ewart G. D., Sutherland T., Gage P. W., Cox G. B. The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels. J. Virol. 70:1996;7108-7115.
    • (1996) J. Virol. , vol.70 , pp. 7108-7115
    • Ewart, G.D.1    Sutherland, T.2    Gage, P.W.3    Cox, G.B.4
  • 16
    • 0030891182 scopus 로고    scopus 로고
    • Ion channels formed by HIV-1 Vpu: A modelling and simulation study
    • Grice A., Kerr I. D., Sansom M. S. P. Ion channels formed by HIV-1 Vpu: A modelling and simulation study. FEBS Lett. 405:1997;299-304.
    • (1997) FEBS Lett. , vol.405 , pp. 299-304
    • Grice, A.1    Kerr, I.D.2    Sansom, M.S.P.3
  • 17
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay A. J., Wolstenholme A. J., Skehel J. J., Smith M. H. The molecular basis of the specific anti-influenza action of amantadine. EMBO J. 4:1985;3021-3024.
    • (1985) EMBO J. , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 18
    • 0026664025 scopus 로고
    • Unpacking the incoming influenza virus
    • Helenius A. Unpacking the incoming influenza virus. Cell. 69:1992;577-578.
    • (1992) Cell , vol.69 , pp. 577-578
    • Helenius, A.1
  • 21
    • 0026761782 scopus 로고
    • Modeling of the structure of bacteriorhodopsin: A molecular dynamics study
    • Jähnig F., Edholm O. Modeling of the structure of bacteriorhodopsin: A molecular dynamics study. J. Mol. Biol. 226:1992;837-850.
    • (1992) J. Mol. Biol. , vol.226 , pp. 837-850
    • Jähnig, F.1    Edholm, O.2
  • 23
    • 0029920368 scopus 로고    scopus 로고
    • Molecular modelling of staphylococcal δ-toxin ion channels by restrained molecular dynamics
    • Kerr I. D., Doak D. G., Sankararamakrishnan R., Breed J., Sansom M. S. P. Molecular modelling of staphylococcal δ-toxin ion channels by restrained molecular dynamics. Protein Eng. 9:1996;161-171.
    • (1996) Protein Eng. , vol.9 , pp. 161-171
    • Kerr, I.D.1    Doak, D.G.2    Sankararamakrishnan, R.3    Breed, J.4    Sansom, M.S.P.5
  • 24
    • 0028070549 scopus 로고
    • Parallel helix bundles and ion channels: Molecular modelling via simulated annealing and restrained molecular dynamics
    • Kerr I. D., Sankararamakrishnan R., Smart O. S., Sansom M. S. P. Parallel helix bundles and ion channels: Molecular modelling via simulated annealing and restrained molecular dynamics. Biophys. J. 67:1994;1501-1515.
    • (1994) Biophys. J. , vol.67 , pp. 1501-1515
    • Kerr, I.D.1    Sankararamakrishnan, R.2    Smart, O.S.3    Sansom, M.S.P.4
  • 25
    • 0001156338 scopus 로고
    • Heterogeneous diffusion of water at protein surfaces: Application to BPTI
    • Knapp E. W., Muegge I. Heterogeneous diffusion of water at protein surfaces: Application to BPTI. J. Phys. Chem. 97:1993;11339-11343.
    • (1993) J. Phys. Chem. , vol.97 , pp. 11339-11343
    • Knapp, E.W.1    Muegge, I.2
  • 28
    • 0343167724 scopus 로고    scopus 로고
    • Structural characterization of the M2 transmembrane peptide backbone using solid state NMR
    • Kovacs F. A., Brenneman M. T., Quine J., Cross T. A. Structural characterization of the M2 transmembrane peptide backbone using solid state NMR. Biophys. J. 72:1997;A399.
    • (1997) Biophys. J. , vol.72 , pp. 399
    • Kovacs, F.A.1    Brenneman, M.T.2    Quine, J.3    Cross, T.A.4
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystalogr. 24:1991;946-950.
    • (1991) J. Appl. Crystalogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0031550769 scopus 로고    scopus 로고
    • Do Vpu and Vpr of human immunodeficiency virus type 1 and NB of influenza B virus have ion channel activities in the viral life cycle?
    • Lamb R. A., Pinto L. H. Do Vpu and Vpr of human immunodeficiency virus type 1 and NB of influenza B virus have ion channel activities in the viral life cycle? Virology. 229:1997;1-24.
    • (1997) Virology , vol.229 , pp. 1-24
    • Lamb, R.A.1    Pinto, L.H.2
  • 33
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear J. D., Wasserman Z. R., DeGrado W. F. Synthetic amphiphilic peptide models for protein ion channels. Science. 240:1988;1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    Degrado, W.F.3
  • 34
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel?
    • Malashkevich V. N., Kammerer R. A., Efimov V. P., Schulthess T., Engel J. The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel? Science. 274:1996;761-765.
    • (1996) Science , vol.274 , pp. 761-765
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.P.3    Schulthess, T.4    Engel, J.5
  • 35
    • 0027390459 scopus 로고
    • Insertion of peptide chains into lipid membranes: An off-lattice Monte Carlo dynamics model
    • Milik M., Skolnick J. Insertion of peptide chains into lipid membranes: An off-lattice Monte Carlo dynamics model. Proteins Struct. Funct. Genet. 15:1993;10-25.
    • (1993) Proteins Struct. Funct. Genet. , vol.15 , pp. 10-25
    • Milik, M.1    Skolnick, J.2
  • 36
    • 0029099311 scopus 로고
    • A Monte Carlo model of fd and Pf1 coat proteins in lipid membranes
    • Milik M., Skolnick J. A Monte Carlo model of fd and Pf1 coat proteins in lipid membranes. Biophys. J. 69:1995;1382-1386.
    • (1995) Biophys. J. , vol.69 , pp. 1382-1386
    • Milik, M.1    Skolnick, J.2
  • 37
    • 0030457853 scopus 로고    scopus 로고
    • Molecular dynamics simulations of ion channels formed by bundles of amphipathic α-helical peptides
    • Mitton P., Sansom M. S. P. Molecular dynamics simulations of ion channels formed by bundles of amphipathic α-helical peptides. Eur. Biophys. J. 25:1996;139-150.
    • (1996) Eur. Biophys. J. , vol.25 , pp. 139-150
    • Mitton, P.1    Sansom, M.S.P.2
  • 38
    • 0029150299 scopus 로고
    • Design of molecular function: Channels of communication
    • Montal M. Design of molecular function: Channels of communication. Annu. Rev. Biophys. Biomol. Struct. 24:1995;31-57.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 31-57
    • Montal, M.1
  • 39
    • 0025913646 scopus 로고
    • Automated modelling of coiled coils: Application to the GCN4 dimerization region
    • Nilges M., Brünger A. T. Automated modelling of coiled coils: Application to the GCN4 dimerization region. Protein Eng. 4:1991;649-659.
    • (1991) Protein Eng. , vol.4 , pp. 649-659
    • Nilges, M.1    Brünger, A.T.2
  • 40
    • 0025135113 scopus 로고
    • Bundles of amphipathic transmembrane α-helices as a structural motif for ion conducting channel proteins: Studies on sodium channels and acetylcholine receptors
    • Oiki S., Madison V., Montal M. Bundles of amphipathic transmembrane α-helices as a structural motif for ion conducting channel proteins: Studies on sodium channels and acetylcholine receptors. Proteins Struct. Funct. Genet. 8:1990;226-236.
    • (1990) Proteins Struct. Funct. Genet. , vol.8 , pp. 226-236
    • Oiki, S.1    Madison, V.2    Montal, M.3
  • 41
    • 0026502806 scopus 로고
    • Oligomeric organization and strain-specific proteolytic modification of the virion M2 protein of influenza A H1N1 viruses
    • Panayotov P. P., Schlesinger R. W. Oligomeric organization and strain-specific proteolytic modification of the virion M2 protein of influenza A H1N1 viruses. Virology. 186:1992;352-355.
    • (1992) Virology , vol.186 , pp. 352-355
    • Panayotov, P.P.1    Schlesinger, R.W.2
  • 43
    • 0029038155 scopus 로고
    • Understanding the mechanism of action of the anti-influenza virus drug amantadine
    • Pinto L. H., Lamb R. A. Understanding the mechanism of action of the anti-influenza virus drug amantadine. Trends Microbiol. 3:1995;271.
    • (1995) Trends Microbiol. , vol.3 , pp. 271
    • Pinto, L.H.1    Lamb, R.A.2
  • 44
    • 0007538854 scopus 로고    scopus 로고
    • The active oligomeric state of the influenza virus M2 ion channel is a tetramer
    • Pinto L. H., Tu Q., Sakeguchi T., Gandhi C., Lamb R. A. The active oligomeric state of the influenza virus M2 ion channel is a tetramer. Biophys. J. 72:1997;A109.
    • (1997) Biophys. J. , vol.72 , pp. 109
    • Pinto, L.H.1    Tu, Q.2    Sakeguchi, T.3    Gandhi, C.4    Lamb, R.A.5
  • 46
    • 0025882246 scopus 로고
    • Ion transport in a model gramicidin channel: Structure and thermodynamics
    • Roux B., Karplus M. Ion transport in a model gramicidin channel: Structure and thermodynamics. Biophys. J. 59:1991;961-981.
    • (1991) Biophys. J. , vol.59 , pp. 961-981
    • Roux, B.1    Karplus, M.2
  • 47
    • 0029775587 scopus 로고    scopus 로고
    • Ab initio molecular dynamics study of proton transfer in a polyglycine analog of the ion channel gramicidin
    • Sagnella D. E., Laason K., Klein M. L. Ab initio molecular dynamics study of proton transfer in a polyglycine analog of the ion channel gramicidin. Biophys. J. 71:1996;1172-1178.
    • (1996) Biophys. J. , vol.71 , pp. 1172-1178
    • Sagnella, D.E.1    Laason, K.2    Klein, M.L.3
  • 48
    • 0029813087 scopus 로고    scopus 로고
    • The pore domain of the nicotinic acetylcholine receptor: Molecular modelling and electrostatics
    • Sankararamakrishnan R., Adcock C., Sansom M. S. P. The pore domain of the nicotinic acetylcholine receptor: Molecular modelling and electrostatics. Biophys. J. 71:1996;1659-1671.
    • (1996) Biophys. J. , vol.71 , pp. 1659-1671
    • Sankararamakrishnan, R.1    Adcock, C.2    Sansom, M.S.P.3
  • 49
    • 0025935264 scopus 로고
    • The biophysics of peptide models of ion channels
    • Sansom M. S. P. The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 55:1991;139-236.
    • (1991) Prog. Biophys. Mol. Biol. , vol.55 , pp. 139-236
    • Sansom, M.S.P.1
  • 50
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols
    • Sansom M. S. P. Structure and function of channel-forming peptaibols. Q. Rev. Biophys. 26:1993;365-421.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 365-421
    • Sansom, M.S.P.1
  • 51
    • 0027339698 scopus 로고
    • Influenza virus M2 protein: A molecular modelling study of the ion channel
    • Sansom M. S. P., Kerr I. D. Influenza virus M2 protein: A molecular modelling study of the ion channel. Protein Eng. 6:1993;65-74.
    • (1993) Protein Eng. , vol.6 , pp. 65-74
    • Sansom, M.S.P.1    Kerr, I.D.2
  • 52
    • 0028631914 scopus 로고
    • Functional reconstitution in lipid vesicles of influenza virus M2 protein expressed by baculovirus: Evidence for proton transfer activity
    • Schroeder C., Ford C. M., Wharton S. A., Hay A. J. Functional reconstitution in lipid vesicles of influenza virus M2 protein expressed by baculovirus: Evidence for proton transfer activity. J. Gen. Virol. 75:1994;3477-3484.
    • (1994) J. Gen. Virol. , vol.75 , pp. 3477-3484
    • Schroeder, C.1    Ford, C.M.2    Wharton, S.A.3    Hay, A.J.4
  • 53
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • Schubert U., Ferrer-Montiel A. V., Oblatt-Montal M., Henklein P., Strebel K., Montal M. Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 398:1996;12-18.
    • (1996) FEBS Lett. , vol.398 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 55
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue R. J., Hay A. J. Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel. Virology. 180:1991;617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 57
    • 0028175436 scopus 로고
    • A method for α-helical integral membrane protein fold prediction
    • Taylor W. R., Jones D. T., Green N. M. A method for α-helical integral membrane protein fold prediction. Proteins Struct. Funct. Genet. 18:1994;281-294.
    • (1994) Proteins Struct. Funct. Genet. , vol.18 , pp. 281-294
    • Taylor, W.R.1    Jones, D.T.2    Green, N.M.3
  • 60
    • 0024848780 scopus 로고
    • The structure of ion channels in membranes of excitable cells
    • Unwin N. The structure of ion channels in membranes of excitable cells. Neuron. 3:1989;665-676.
    • (1989) Neuron , vol.3 , pp. 665-676
    • Unwin, N.1
  • 61
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature. 373:1995;37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 63
    • 0028980598 scopus 로고
    • Activation of the M2 ion channel of influenza virus: A role for the transmembrane domain histidine residue
    • Wang C., Lamb R. A., Pinto L. H. Activation of the M2 ion channel of influenza virus: A role for the transmembrane domain histidine residue. Biophys. J. 69:1995;1363-1371.
    • (1995) Biophys. J. , vol.69 , pp. 1363-1371
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 65
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid-protein interactions - A molecular-dynamics study of the gramicidin-A channel in a DMPC bilayer
    • Woolf T. B., Roux B. Structure, energetics, and dynamics of lipid-protein interactions - A molecular-dynamics study of the gramicidin-A channel in a DMPC bilayer. Proteins Struct. Funct. Genet. 24:1996;92-114.
    • (1996) Proteins Struct. Funct. Genet. , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.