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Volumn 92, Issue 12, 2007, Pages 4335-4343

Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza A virus

Author keywords

[No Author keywords available]

Indexed keywords

AMANTADINE; MONOMER; PROTON; TETRAMER;

EID: 34250334756     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.090183     Document Type: Article
Times cited : (173)

References (52)
  • 2
    • 85030506773 scopus 로고    scopus 로고
    • Morbidity and Mortality Weekly Report. 2006. High levels of adamantane resistance among Influenza A (H3N2) viruses and interim guidelines for use of antiviral agents. United States, 2005-06 Influenza season. Dispatch 55, January 26.
    • Morbidity and Mortality Weekly Report. 2006. High levels of adamantane resistance among Influenza A (H3N2) viruses and interim guidelines for use of antiviral agents. United States, 2005-06 Influenza season. Dispatch 55, January 26.
  • 3
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: Characterization of the amantadine block
    • Wang, C., K. Takeuchi, L. H. Pinto, and R. A. Lamb. 1993. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J. Virol. 67:5585-5594.
    • (1993) J. Virol , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 4
    • 0028100022 scopus 로고
    • Direct measurement of the influenza A virus protein ion channel activity in mammalian cells
    • Wang, C., R. A. Lamb, and L. H. Pinto. 1994. Direct measurement of the influenza A virus protein ion channel activity in mammalian cells. Virology. 205:133-140.
    • (1994) Virology , vol.205 , pp. 133-140
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 6
    • 0026785994 scopus 로고
    • The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
    • Duff, K. C., and R. H. Ashley. 1992. The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers. Virology. 190:485-489.
    • (1992) Virology , vol.190 , pp. 485-489
    • Duff, K.C.1    Ashley, R.H.2
  • 7
    • 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) J. Am. Chem. Soc , vol.128 , pp. 7242-7251
    • Luo, W.1    Hong, M.2
  • 8
    • 0026745087 scopus 로고
    • The secondary structure of influenza A M2 transmembrane domain. A circular dichroism study
    • Duff, K. C., S. M. Kelly, N. C. Price, and J. P. Bradshaw. 1992. The secondary structure of influenza A M2 transmembrane domain. A circular dichroism study. FEBS Lett. 311:256-258.
    • (1992) FEBS Lett , vol.311 , pp. 256-258
    • Duff, K.C.1    Kelly, S.M.2    Price, N.C.3    Bradshaw, J.P.4
  • 9
    • 33646494326 scopus 로고    scopus 로고
    • Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity
    • Hu, J., R. Fu, K. Nishimura, L. Zhang, H.-X. Zhou, D. D. Busath, V. Vijayvergiya, and T. A. Cross. 2006. Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity. Proc. Natl. Acad. Sci. USA. 103:6865-6870.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6865-6870
    • Hu, J.1    Fu, R.2    Nishimura, K.3    Zhang, L.4    Zhou, H.-X.5    Busath, D.D.6    Vijayvergiya, V.7    Cross, T.A.8
  • 10
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane four-helix bundle of influenza A M2 protein channel: Structural implications from helix tilt and orientation
    • Kovacs, F. A., and T. A. Cross. 1997. Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation. Biophys. J. 73:2511-2517.
    • (1997) Biophys. J , vol.73 , pp. 2511-2517
    • Kovacs, F.A.1    Cross, T.A.2
  • 11
    • 0037027306 scopus 로고    scopus 로고
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR. Biochemistry. 41:13170-13177.
    • (2002) Biochemistry , vol.41 , pp. 13170-13177
    • Nishimura, K.1    Kim, S.2    Zhang, L.3    Cross, T.A.4
  • 12
    • 28844493428 scopus 로고    scopus 로고
    • + channel: The gating mechanism of influenza A M2
    • + channel: the gating mechanism of influenza A M2. Structure. 13:1789-1798.
    • (2005) Structure , vol.13 , pp. 1789-1798
    • Kass, I.1    Arkin, I.T.2
  • 13
    • 25844476272 scopus 로고    scopus 로고
    • A computational study of the closed and open states of the influenza a M2 proton channel
    • Wu, Y., and G. A. Voth. 2005. A computational study of the closed and open states of the influenza a M2 proton channel. Biophys. J. 89:2402-2411.
    • (2005) Biophys. J , vol.89 , pp. 2402-2411
    • Wu, Y.1    Voth, G.A.2
  • 15
    • 0037131381 scopus 로고    scopus 로고
    • The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue
    • Tang, Y., F. Zaitseva, R. A. Lamb, and L. H. Pinto. 2002. The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J. Biol. Chem. 277:39880-39886.
    • (2002) J. Biol. Chem , vol.277 , pp. 39880-39886
    • Tang, Y.1    Zaitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 16
    • 0029038155 scopus 로고
    • Understanding the mechanism of action of the anti-influenza virus drug amantadine
    • Pinto, L. H., and R. A. Lamb. 1995. Understanding the mechanism of action of the anti-influenza virus drug amantadine. Trends Microbiol. 3:271.
    • (1995) Trends Microbiol , vol.3 , pp. 271
    • Pinto, L.H.1    Lamb, R.A.2
  • 17
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian, C., P. F. Gao, L. H. Pinto, R. A. Lamb, and T. A. Cross. 2003. Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers. Protein Sci. 12:2597-2605.
    • (2003) Protein Sci , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, P.F.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 18
    • 0002988267 scopus 로고
    • The action of adamantanamines against influenza A viruses: Inhibition of the M2 ion channel protein
    • Hay, A. J. 1992. The action of adamantanamines against influenza A viruses: inhibition of the M2 ion channel protein. Semin. Virol. 3:21-30.
    • (1992) Semin. Virol , vol.3 , pp. 21-30
    • Hay, A.J.1
  • 19
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue, R. J., and A. J. Hay. 1991. Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology. 180:617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 20
    • 0027339698 scopus 로고
    • Influenza virus M2 protein: A molecular modeling study of the ion channel
    • Sansom, M. S., and I. D. Kerr. 1993. Influenza virus M2 protein: a molecular modeling study of the ion channel. Protein Eng. 6:65-74.
    • (1993) Protein Eng , vol.6 , pp. 65-74
    • Sansom, M.S.1    Kerr, I.D.2
  • 21
    • 14144251553 scopus 로고    scopus 로고
    • Sequence determinants of a transmembrane proton channel: An inverse relationship between stability and function
    • Stouffer, A. L., V. Nanda, J. D. Lear, and W. F. DeGrado. 2005. Sequence determinants of a transmembrane proton channel: an inverse relationship between stability and function. J. Mol. Biol. 347:169-179.
    • (2005) J. Mol. Biol , vol.347 , pp. 169-179
    • Stouffer, A.L.1    Nanda, V.2    Lear, J.D.3    DeGrado, W.F.4
  • 22
    • 33646494326 scopus 로고    scopus 로고
    • Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity
    • Hu, J., R. Fu, K. Nishimura, L. Zhang, H. X. Zhou, D. D. Busath, V. Vijayvergiya, and T. A. Cross. 2006. Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity. Proc. Natl. Acad. Sci. USA. 103:6865-6870.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6865-6870
    • Hu, J.1    Fu, R.2    Nishimura, K.3    Zhang, L.4    Zhou, H.X.5    Busath, D.D.6    Vijayvergiya, V.7    Cross, T.A.8
  • 24
    • 1842427673 scopus 로고    scopus 로고
    • A novel method of resistance for influenza against a channel-blocking antiviral drug
    • Astrahan, P., I. Kass, M. A. Cooper, and I. T. Arkin. 2004. A novel method of resistance for influenza against a channel-blocking antiviral drug. Proteins. 55:251-257.
    • (2004) Proteins , vol.55 , pp. 251-257
    • Astrahan, P.1    Kass, I.2    Cooper, M.A.3    Arkin, I.T.4
  • 25
    • 0034700255 scopus 로고    scopus 로고
    • pH-Dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus
    • Salom, D., B. R. Hill, J. D. Lear, and W. F. DeGrado. 2000. pH-Dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus. Biochemistry. 39:14160-14170.
    • (2000) Biochemistry , vol.39 , pp. 14160-14170
    • Salom, D.1    Hill, B.R.2    Lear, J.D.3    DeGrado, W.F.4
  • 27
    • 33846595904 scopus 로고
    • High-resolution heteronuclear dipolar solid-state NMR spectroscopy
    • Wu, C. H., A. Ramamoorthy, and S. J. Opella. 1994. High-resolution heteronuclear dipolar solid-state NMR spectroscopy. J. Magn. Reson. A. 109:270-272.
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 29
    • 0032578027 scopus 로고    scopus 로고
    • Phases and phase transitions of the phosphatidylcholines
    • Koynova, R., and M. Caffrey. 1998. Phases and phase transitions of the phosphatidylcholines. Biochim. Biophys. Acta Rev. Biomembr. 1376:91-145.
    • (1998) Biochim. Biophys. Acta Rev. Biomembr , vol.1376 , pp. 91-145
    • Koynova, R.1    Caffrey, M.2
  • 30
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for x-ray protein-structure refinement
    • Engh, R. A., and R. Huber. 1991. Accurate bond and angle parameters for x-ray protein-structure refinement. Acta Crystallogr. A. 47:392-400.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 31
    • 0035819626 scopus 로고    scopus 로고
    • Orientation of amide-nitrogen-15 chemical shift tensors in peptides: A quantum chemical study
    • Brender, J. R., D. M. Taylor, and A. Ramamoorthy. 2001. Orientation of amide-nitrogen-15 chemical shift tensors in peptides: a quantum chemical study. J. Am. Chem. Soc. 123:914-923.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 914-923
    • Brender, J.R.1    Taylor, D.M.2    Ramamoorthy, A.3
  • 34
    • 0030698391 scopus 로고    scopus 로고
    • π-histidine side chains determined by three-dimensional solid-state NMR spectroscopy of polycrystalline samples
    • π-histidine side chains determined by three-dimensional solid-state NMR spectroscopy of polycrystalline samples. J. Am. Chem. Soc. 119:10479-10486.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 10479-10486
    • Ramamoorthy, A.1    Wu, C.H.2    Opella, S.J.3
  • 36
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from influenza A virus: An intrinsic property
    • Kovacs, F. A., J. K. Denny, Z. Song, J. R. Quine, and T. A. Cross. 2000. Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property. J. Mol. Biol. 295:117-125.
    • (2000) J. Mol. Biol , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.K.2    Song, Z.3    Quine, J.R.4    Cross, T.A.5
  • 37
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • Marassi, F. M., and S. J. Opella. 2000. A solid-state NMR index of helical membrane protein structure and topology. J. Magn. Reson. 144:150-155.
    • (2000) J. Magn. Reson , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 38
    • 0042029753 scopus 로고    scopus 로고
    • Dipolar waves as NMR maps of helices in proteins
    • Mesleh, M. F., and S. J. Opella. 2003. Dipolar waves as NMR maps of helices in proteins. J. Magn. Reson. 163:288-299.
    • (2003) J. Magn. Reson , vol.163 , pp. 288-299
    • Mesleh, M.F.1    Opella, S.J.2
  • 40
    • 85030519097 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 41
    • 85030519343 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 42
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Canutescu, A. A., A. A. Shelenkov, and R. L. Dunbrack. 2003. A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci. 12:2001-2004.
    • (2003) Protein Sci , vol.12 , pp. 2001-2004
    • Canutescu, A.A.1    Shelenkov, A.A.2    Dunbrack, R.L.3
  • 45
    • 0036100338 scopus 로고    scopus 로고
    • An improved hydrogen bond potential: Impact on medium resolution protein structures
    • Fabiola, F., R. Bertram, A. Korostelev, and M. S. Chapman. 2002. An improved hydrogen bond potential: impact on medium resolution protein structures. Protein Sci. 11:1415-1423.
    • (2002) Protein Sci , vol.11 , pp. 1415-1423
    • Fabiola, F.1    Bertram, R.2    Korostelev, A.3    Chapman, M.S.4
  • 46
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean and eukaryotic organisms
    • Wallin, E., and G. von Heijne. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean and eukaryotic organisms. Protein Sci. 7:1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 47
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens, T. J., and I. T. Arkin. 2000. Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins. 39:417-420.
    • (2000) Proteins , vol.39 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 48
    • 0028280706 scopus 로고
    • Four helix bundle diversity in globular proteins
    • Harris, N. L., S. R. Presnell, and F. E. Cohen. 1994. Four helix bundle diversity in globular proteins. J. Mol. Biol. 236:1356-1368.
    • (1994) J. Mol. Biol , vol.236 , pp. 1356-1368
    • Harris, N.L.1    Presnell, S.R.2    Cohen, F.E.3
  • 49
    • 0037172965 scopus 로고    scopus 로고
    • Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein
    • Howard, K. P., J. D. Lear, and W. F. DeGrado. 2002. Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein. Proc. Natl. Acad. Sci. USA. 99:8568-8572.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8568-8572
    • Howard, K.P.1    Lear, J.D.2    DeGrado, W.F.3
  • 51
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., J. H. Prestegard, and D. M. Engelman. 1997. A transmembrane helix dimer: structure and implications. Science. 276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 52
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • Duong-Ly, K. C., V. Nanda, W. F. DeGrado, and K. P. Howard. 2005. The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci. 14:856-861.
    • (2005) Protein Sci , vol.14 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    DeGrado, W.F.3    Howard, K.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.