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Volumn 463, Issue 7281, 2010, Pages 689-692

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

AMANTADINE; ANTIVIRUS AGENT; CARBON 13; MEMBRANE PROTEIN; PROTEIN M2; PROTON; SYNTHETIC PEPTIDE; VIRUS PROTEIN;

EID: 76249125649     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08722     Document Type: Article
Times cited : (540)

References (30)
  • 1
    • 68249121326 scopus 로고    scopus 로고
    • Structure and function of the influenza M2 proton channel
    • Cady, S. D., Luo, W. B., Hu, F. & Hong, M. Structure and function of the influenza M2 proton channel. Biochemistry 48, 7356-7364 (2009).
    • (2009) Biochemistry , vol.48 , pp. 7356-7364
    • Cady, S.D.1    Luo, W.B.2    Hu, F.3    Hong, M.4
  • 2
    • 38749151911 scopus 로고    scopus 로고
    • Structural basis for the function and inhibition of an influenza virus proton channel
    • Stouffer, A. L., et al. Structural basis for the function and inhibition of an influenza virus proton channel. Nature 451, 596-599 (2008).
    • (2008) Nature , vol.451 , pp. 596-599
    • Stouffer, A.L.1
  • 3
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus.
    • Schnell, J. R. & Chou, J. J. Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451, 591-595 (2008).
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 4
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of influenza A and B viruses.
    • Pinto, L. H. & Lamb, R. A. The M2 proton channels of influenza A and B viruses. J. Biol. Chem. 281, 8997-9000 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 5
    • 0034700255 scopus 로고    scopus 로고
    • PH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus
    • Salom, D., Hill, B. R., Lear, J. D. & DeGrado, W. F. pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus. Biochemistry 39, 14160-14170 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14160-14170
    • Salom, D.1    Hill, B.R.2    Lear, J.D.3    Degrado, W.4
  • 6
    • 33744941313 scopus 로고    scopus 로고
    • 1H-driven spin diffusion NMR spectroscopy.
    • 1H-driven spin diffusion NMR spectroscopy. J. Am. Chem. Soc. 128, 7242-7251 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7242-7251
    • Luo, W.1    Hong, M.2
  • 7
    • 46049110693 scopus 로고    scopus 로고
    • The interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus
    • Stouffer, A. L., et al. The interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus. Structure 16, 1067-1076 (2008).
    • (2008) Structure , vol.16 , pp. 1067-1076
    • Stouffer, A.L.1
  • 8
    • 67650018858 scopus 로고    scopus 로고
    • Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel.
    • Ma, C., et al. Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel. Proc. Natl Acad. Sci. USA 106, 12283-12288 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 12283-12288
    • Ma, C.1
  • 9
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: Characterization of the amantadine block
    • Wang, C., Takeuchi, K., Pinto, L. H. & Lamb, R. A. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J. Virol. 67, 5585-5594 (1993).
    • (1993) J. Virol. , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 10
    • 49449093199 scopus 로고    scopus 로고
    • Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel.
    • Jing, X., et al. Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel. Proc. Natl Acad. Sci. USA 105, 10967-10972 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 10967-10972
    • Jing, X.1
  • 11
    • 0028181687 scopus 로고
    • Influenza A virus M2 ion channel protein: A structure-function analysis
    • Holsinger, L. J., Nichani, D., Pinto, L. H. & Lamb, R. A. Influenza A virus M2 ion channel protein: a structure-function analysis. J. Virol. 68, 1551-1563 (1994).
    • (1994) J. Virol. , vol.68 , pp. 1551-1563
    • Holsinger, L.J.1    Nichani, D.2    Pinto, L.H.3    Lamb, R.A.4
  • 12
    • 45149145322 scopus 로고
    • Rotational echo double resonance NMR.
    • Gullion, T. & Schaefer, J. Rotational echo double resonance NMR. J. Magn. Reson. 81, 196-200 (1989).
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 13
    • 34848868442 scopus 로고    scopus 로고
    • Sidechain conformation and gating of the M2 transmembrane peptide proton channel of influenza A virus from solid-state NMR.
    • Luo, W., Mani, R. & Hong, M. Sidechain conformation and gating of the M2 transmembrane peptide proton channel of influenza A virus from solid-state NMR. J. Phys. Chem. 111, 10825-10832 (2007).
    • (2007) J. Phys. Chem. , vol.111 , pp. 10825-10832
    • Luo, W.1    Mani, R.2    Hong, M.3
  • 15
    • 58149345493 scopus 로고    scopus 로고
    • Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: The role of Ser31 in amantadine binding.
    • Cady, S. D., Mishanina, T. V. & Hong, M. Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: the role of Ser31 in amantadine binding. J. Mol. Biol. 385, 1127-1141 (2009).
    • (2009) J. Mol. Biol. , vol.385 , pp. 1127-1141
    • Cady, S.D.1    Mishanina, T.V.2    Hong, M.3
  • 16
    • 38949181061 scopus 로고    scopus 로고
    • Solid-state NMR and MD simulations of the antiviral drug amantadine solubilized in DMPC bilayers.
    • Li, C., Yi, M., Hu, J., Zhou, H. X. & Cross, T. A. Solid-state NMR and MD simulations of the antiviral drug amantadine solubilized in DMPC bilayers. Biophys. J. 94, 1295-1302 (2008).
    • (2008) Biophys. J. , vol.94 , pp. 1295-1302
    • Li, C.1    Yi, M.2    Hu, J.3    Zhou, H.X.4    Cross, T.A.5
  • 17
    • 49149107480 scopus 로고    scopus 로고
    • A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine.
    • Yi, M., Cross, T. A. & Zhou, H. X. A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine. J. Phys. Chem. B 112, 7977-7979 (2008).
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7977-7979
    • Yi, M.1    Cross, T.A.2    Zhou, H.X.3
  • 18
    • 36549041108 scopus 로고    scopus 로고
    • Proton transport behavior through the influenza A M2 channel: Insights from molecular simulation
    • Chen, H., Wu, Y. & Voth, G. A. Proton transport behavior through the influenza A M2 channel: insights from molecular simulation. Biophys. J. 93, 3470-3479 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 3470-3479
    • Chen, H.1    Wu, Y.2    Voth, G.A.3
  • 19
    • 0001043711 scopus 로고    scopus 로고
    • 2D dipolar couplings with a universal REDOR dephasing curve.
    • 2D dipolar couplings with a universal REDOR dephasing curve. J. Magn. Reson. 146, 220-222 (2000).
    • (2000) J. Magn. Reson. , vol.146 , pp. 220-222
    • Gullion, T.1
  • 20
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza A virus
    • Hu, J., et al. Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza A virus. Biophys. J. 92, 4335-4343 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 4335-4343
    • Hu, J.1
  • 21
    • 0037131381 scopus 로고    scopus 로고
    • The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue.
    • Tang, Y., Zaitseva, F., Lamb, R. A. & Pinto, L. H. The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J. Biol. Chem. 277, 39880-39886 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39880-39886
    • Tang, Y.1    Zaitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 22
    • 34447258592 scopus 로고    scopus 로고
    • The chemical and dynamical influence of the antiviral drug amantadine on the M2 proton channel transmembrane domain
    • Hu, J., Riqiang, F. & Cross, T. A. The chemical and dynamical influence of the antiviral drug amantadine on the M2 proton channel transmembrane domain. Biophys. J. 93, 276-283 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 276-283
    • Hu, J.1    Riqiang, F.2    Cross, T.A.3
  • 23
    • 0345598917 scopus 로고    scopus 로고
    • Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers.
    • Cristian, L., Lear, J. D. & DeGrado, W. F. Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers. Proc. Natl Acad. Sci. USA 100, 14772-14777 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 14772-14777
    • Cristian, L.1    Lear, J.D.2    Degrado, W.F.3
  • 24
    • 36849047240 scopus 로고    scopus 로고
    • Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.
    • Li, C., Qin, H., Gao, F. P. & Cross, T. A. Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel. Biochim. Biophys. Acta 1768, 3162-3170 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3162-3170
    • Li, C.1    Qin, H.2    Gao, F.P.3    Cross, T.A.4
  • 25
    • 40349105892 scopus 로고    scopus 로고
    • Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel.
    • Cady, S. D. & Hong, M. Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel. Proc. Natl Acad. Sci. USA 105, 1483-1488 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 1483-1488
    • Cady, S.D.1    Hong, M.2
  • 26
    • 0030934244 scopus 로고    scopus 로고
    • Different modes of inhibition by adamantane amine derivatives and natural polyamines of the functionally reconstituted influenza virus M2 proton channel protein.
    • Lin, T. I., Heider, H. & Schroeder, C. Different modes of inhibition by adamantane amine derivatives and natural polyamines of the functionally reconstituted influenza virus M2 proton channel protein. J. Gen. Virol. 78, 767-774 (1997).
    • (1997) J. Gen. Virol. , vol.78 , pp. 767-774
    • Lin, T.I.1    Heider, H.2    Schroeder, C.3
  • 27
    • 67650540781 scopus 로고    scopus 로고
    • Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus.
    • Wang, J., et al. Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus. J. Am. Chem. Soc. 131, 8066-8076 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8066-8076
    • Wang, J.1
  • 28
    • 67650080518 scopus 로고    scopus 로고
    • Immobilization of the influenza A M2 transmembrane peptide in virus-envelope mimetic lipid membranes: A solid-state NMR investigation
    • Luo, W., Cady, S. D. & Hong, M. Immobilization of the influenza A M2 transmembrane peptide in virus-envelope mimetic lipid membranes: a solid-state NMR investigation. Biochemistry 48, 6361-6368 (2009).
    • (2009) Biochemistry , vol.48 , pp. 6361-6368
    • Luo, W.1    Cady, S.D.2    Hong, M.3
  • 29
    • 67650547197 scopus 로고    scopus 로고
    • 13C chemical shifts by solid-state NMR for the determination of protein sidechain conformation: The influenza M2 transmembrane peptide as an example.
    • 13C chemical shifts by solid-state NMR for the determination of protein sidechain conformation: the influenza M2 transmembrane peptide as an example. J. Am. Chem. Soc. 131, 7806-7816 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7806-7816
    • Hong, M.1    Mishanina, T.V.2    Cady, S.D.3
  • 30
    • 0001853326 scopus 로고    scopus 로고
    • Deuterium REDOR: Principles and applications for distance measurements.
    • Sack, I., Goldbourt, A., Vega, S. & Buntkowsky, G. Deuterium REDOR: principles and applications for distance measurements. J. Magn. Reson. 138, 54-65 (1999).
    • (1999) J. Magn. Reson. , vol.138 , pp. 54-65
    • Sack, I.1    Goldbourt, A.2    Vega, S.3    Buntkowsky, G.4


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