메뉴 건너뛰기




Volumn 106, Issue 32, 2009, Pages 13311-13316

Conformational heterogeneity of the M2 proton channel and a structural model for channel activation

Author keywords

Amantadine; Helix kink; Histidine tetrad; MD simulations; Solid state NMR

Indexed keywords

AMANTADINE; GLYCINE; MEMBRANE PROTEIN; PROTEIN M2; PROTON; TRYPTOPHAN; WATER;

EID: 69549104773     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0906553106     Document Type: Article
Times cited : (101)

References (45)
  • 1
    • 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, et al. (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
  • 2
    • 0037131381 scopus 로고    scopus 로고
    • 2 proton channel is formed by a single tryptophan residue
    • DOI 10.1074/jbc.M206582200
    • Tang Y, Zaitseva F, Lamb RA, Pinto LH (2002) The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J Biol Chem 277:39880-39886. (Pubitemid 35190974)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39880-39886
    • Tang, Y.1    Zaitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 3
    • 20444385829 scopus 로고    scopus 로고
    • Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza a virus
    • DOI 10.1074/jbc.M412406200
    • Venkataraman P, Lamb RA, Pinto LH (2005) Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus. J Biol Chem 280:21463-21472. (Pubitemid 40805711)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21463-21472
    • Venkataraman, P.1    Lamb, R.A.2    Pinto, L.H.3
  • 4
    • 0025923280 scopus 로고
    • Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • Holsinger LJ, Lamb RA (1991) Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183:32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 5
    • 52249123874 scopus 로고    scopus 로고
    • PH-induced conformational change of the influenza M2 protein C-terminal domain
    • Nguyen PA, et al. (2008) pH-induced conformational change of the influenza M2 protein C-terminal domain. Biochemistry 47:9934-9936.
    • (2008) Biochemistry , vol.47 , pp. 9934-9936
    • Nguyen, P.A.1
  • 6
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of influenza a and B viruses
    • Pinto LH, Lamb RA (2006) The M2 proton channels of influenza A and B viruses. J Biol Chem 281:8997-9000.
    • (2006) J Biol Chem , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 7
    • 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. (2008) 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) Proc Natl Acad Sci USA , vol.105 , pp. 10967-10972
    • Jing, X.1
  • 8
    • 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 AL, et al. (2008) The interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus. Structure (London) 16:1067-1076.
    • (2008) Structure (London) , vol.16 , pp. 1067-1076
    • Stouffer, A.L.1
  • 9
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza a virus
    • DOI 10.1529/biophysj.106.090183
    • Hu J, et al. (2007) Backbone structure of the amantadine-blocked transmembrane domain M2 proton channel from influenza A virus. Biophys J 92:4335-4343. (Pubitemid 46915327)
    • (2007) Biophysical Journal , vol.92 , Issue.12 , pp. 4335-4343
    • Hu, J.1    Asbury, T.2    Achuthan, S.3    Li, C.4    Bertram, R.5    Quine, J.R.6    Fu, R.7    Cross, T.A.8
  • 10
    • 0037027306 scopus 로고    scopus 로고
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR
    • DOI 10.1021/bi0262799
    • + channel helical bundle combining precise orientational and distance restraints from solid-state NMR. Biochemistry 41:13170-13177. (Pubitemid 35244706)
    • (2002) Biochemistry , vol.41 , Issue.44 , pp. 13170-13177
    • Nishimura, K.1    Kim, S.2    Zhang, L.3    Cross, T.A.4
  • 11
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza a viruses: Evidence that it forms a tetrameric channel
    • Sugrue RJ, Hay AJ (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
  • 12
    • 0026612385 scopus 로고
    • Influenza-virus M2 protein has ion channel activity
    • Pinto LH, Holsinger LJ, Lamb RA (1992) Influenza-virus M2 protein has ion channel activity. Cell 69:517-528.
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 13
    • 0028980598 scopus 로고
    • Activation of the M2 ion channel of influenza virus: A role for the transmembrane domain histidine residue
    • Wang C, Lamb RA, Pinto LH (1995) Activation of the M2 ion channel of influenza virus: A role for the transmembrane domain histidine residue. Biophys J 69:1363-1371.
    • (1995) Biophys J , vol.69 , pp. 1363-1371
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 16
    • 14144251553 scopus 로고    scopus 로고
    • Sequence determinants of a transmembrane proton channel: An inverse relationship between stability and function
    • DOI 10.1016/j.jmb.2005.01.023
    • Stouffer AL, Nanda V, Lear JD, DeGrado WF (2005) Sequence determinants of a transmembrane proton channel: An inverse relationship between stability and function. J Mol Biol 347:169-179. (Pubitemid 40283637)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.1 , pp. 169-179
    • Stouffer, A.L.1    Nanda, V.2    Lear, J.D.3    Degrado, W.F.4
  • 17
    • 0027339698 scopus 로고
    • 2 protein: A molecular modelling study of the ion channel
    • Sansom MS, Kerr ID (1993) Influenza virus M2 protein: A molecular modeling study of the ion channel. Protein Eng 6:65-74. (Pubitemid 23048942)
    • (1993) Protein Engineering , vol.6 , Issue.1 , pp. 65-74
    • Sansom, M.S.P.1    Kerr, I.D.2
  • 18
    • 36549041108 scopus 로고    scopus 로고
    • Proton transport behavior through the influenza a M2 channel: Insights from molecular simulation
    • DOI 10.1529/biophysj.107.105742
    • Chen H, Wu Y, Voth GA (2007) Proton transport behavior through the influenza AM2 channel: Insights from molecular simulation. Biophys J 93:3470-3479. (Pubitemid 350190810)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3470-3479
    • Chen, H.1    Wu, Y.2    Voth, G.A.3
  • 19
    • 49149107480 scopus 로고    scopus 로고
    • A secondary gate as amechanism for inhibition of the M2 proton channel by amantadine
    • Yi M, Cross TA, Zhou H-X (2008) A secondary gate as amechanism for inhibition of the M2 proton channel by amantadine. J Phys Chem B 112:7977-7979.
    • (2008) J Phys Chem B , vol.112 , pp. 7977-7979
    • Yi, M.1    Cross, T.A.2    Zhou, H.-X.3
  • 20
    • 59049103481 scopus 로고    scopus 로고
    • Molecular dynamics calculations suggest a conduction mechanism for the M2 proton channel from influenza a virus
    • Khurana E, et al. (2009) Molecular dynamics calculations suggest a conduction mechanism for the M2 proton channel from influenza A virus. Proc Natl Acad Sci USA 106:1069-1074.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1069-1074
    • Khurana, E.1
  • 22
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza a virus
    • DOI 10.1038/nature06531, PII NATURE06531
    • Schnell JR, Chou JJ (2008) Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451:591-595. (Pubitemid 351186272)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 23
    • 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 Ser-31 in amantadine binding
    • Cady SD, Mishanina TV, Hong M (2009) Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: The role of Ser-31 in amantadine binding. J Mol Biol 385:1127-1141.
    • (2009) J Mol Biol , vol.385 , pp. 1127-1141
    • Cady, S.D.1    Mishanina, T.V.2    Hong, M.3
  • 24
    • 66149112971 scopus 로고    scopus 로고
    • Mechanism of drug inhibition and drug resistance of influenza a M2 channel
    • Pielak RM, Schnell JR, Chou JJ (2009) Mechanism of drug inhibition and drug resistance of influenza A M2 channel. Proc Natl Acad Sci USA 106:7379-7384.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7379-7384
    • Pielak, R.M.1    Schnell, J.R.2    Chou, J.J.3
  • 25
    • 59649114004 scopus 로고    scopus 로고
    • Gating mechanism of the influenza AM2 channel revealed by 1D and 2D IR spectroscopies
    • Manor J, et al. (2009) Gating mechanism of the influenza AM2 channel revealed by 1D and 2D IR spectroscopies. Structure (London) 17:247-254.
    • (2009) Structure (London) , vol.17 , pp. 247-254
    • Manor, J.1
  • 26
    • 34447258592 scopus 로고    scopus 로고
    • 2 proton channel transmembrane domain
    • DOI 10.1529/biophysj.106.102103
    • Hu J, Fu R, Cross TA (2007) The chemical and dynamical influence of the antiviral drug amantadine on the M2 proton channel transmembrane domain. Biophys J 93:276-283. (Pubitemid 47041672)
    • (2007) Biophysical Journal , vol.93 , Issue.1 , pp. 276-283
    • Hu, J.1    Fu, R.2    Cross, T.A.3
  • 27
    • 36849047240 scopus 로고    scopus 로고
    • Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza a M2 proton channel
    • DOI 10.1016/j.bbamem.2007.08.025, PII S0005273607003367
    • Li C, Qin H, Gao FP, Cross TA (2007) Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel. Biochim Biophys Acta 1768:3162-3170. (Pubitemid 350236087)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.12 , pp. 3162-3170
    • Li, C.1    Qin, H.2    Gao, F.P.3    Cross, T.A.4
  • 28
    • 40349105892 scopus 로고    scopus 로고
    • Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel
    • Cady SD, Hong M (2008) Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel. Proc Natl Acad Sci USA 105:1483-1488.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1483-1488
    • Cady, S.D.1    Hong, M.2
  • 29
    • 0035825634 scopus 로고    scopus 로고
    • The gating mechanism of the large mechanosensitive channel MscL
    • DOI 10.1038/35055559
    • Sukharev S, Betanzos M, Chiang CS, Guy HR (2001) The gating mechanism of the large mechanosensitive channel MscL. Nature 409:720-724. (Pubitemid 32144517)
    • (2001) Nature , vol.409 , Issue.6821 , pp. 720-724
    • Sukharev, S.1    Betanzos, M.2    Chiang, C.-S.3    Robert Guy, H.4
  • 31
    • 50649114379 scopus 로고    scopus 로고
    • Opening the molecular floodgates
    • Gandhi CS, Rees DC (2008) Opening the molecular floodgates. Science 321:1166-1167.
    • (2008) Science , vol.321 , pp. 1166-1167
    • Gandhi, C.S.1    Rees, D.C.2
  • 32
    • 0035918599 scopus 로고    scopus 로고
    • Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza a virus
    • DOI 10.1021/bi0028441
    • Okada A, Miura T, Takeuchi H (2001) Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza A virus. Biochemistry 40:6053-6060. (Pubitemid 32466308)
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 6053-6060
    • Okada, A.1    Miura, T.2    Takeuchi, H.3
  • 33
    • 0347480205 scopus 로고    scopus 로고
    • Studies of structural changes in the M2 proton channel of influenza a virus by tryptophan fluorescence
    • Czabotar PE, Martin SR, Hay AJ (2004) Studies of structural changes in the M2 proton channel of influenza A virus by tryptophan fluorescence. Virus Res 99:57-61.
    • (2004) Virus Res , vol.99 , pp. 57-61
    • Czabotar, P.E.1    Martin, S.R.2    Hay, A.J.3
  • 34
    • 38349105382 scopus 로고    scopus 로고
    • 19F NMR spectroscopy reveals that Trp41 participates in the gating mechanism of the M2 proton channel of influenza a virus
    • 19F NMR spectroscopy reveals that Trp41 participates in the gating mechanism of the M2 proton channel of influenza A virus. J Am Chem Soc 130:918-924.
    • (2008) J Am Chem Soc , vol.130 , pp. 918-924
    • Witter, R.1
  • 36
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie JU (2001) Stabilizing membrane proteins. Curr Opin Struct Biol 11:397-402.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 37
    • 0033073762 scopus 로고    scopus 로고
    • The influenza virus M2 ion channel protein: Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking
    • Bauer CM, Pinto LH, Cross TA, Lamb RA (1999) The influenza virus M2 ion channel protein: Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking. Virology 254:196-209.
    • (1999) Virology , vol.254 , pp. 196-209
    • Bauer, C.M.1    Pinto, L.H.2    Cross, T.A.3    Lamb, R.A.4
  • 38
    • 46149085900 scopus 로고    scopus 로고
    • Spontaneous conformational change and toxin binding in α7 acetylcholine receptor: Insight into channel activation and inhibition
    • DOI 10.1073/pnas.0710530105
    • Yi M, Tjong H, Zhou H-X (2008) Spontaneous conformational change and toxin binding in α7 acetylcholine receptor: Insight into channel activation and inhibition. Proc Natl Acad Sci USA 105:8280-8285. (Pubitemid 351904747)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.24 , pp. 8280-8285
    • Yi, M.1    Tjong, H.2    Zhou, H.-X.3
  • 40
    • 0035085645 scopus 로고    scopus 로고
    • Definitive assignment of proton selectivity and attoampere unitary current to the M2 ion channel protein of influenza a virus
    • Lin TI, Schroeder C (2001) Definitive assignment of proton selectivity and attoampere unitary current to the M2 ion channel protein of influenza A virus. J Virol 75:3647-3656.
    • (2001) J Virol , vol.75 , pp. 3647-3656
    • Lin, T.I.1    Schroeder, C.2
  • 41
    • 0037440103 scopus 로고    scopus 로고
    • Differences in conductance of M2 proton channels of two influenza viruses at low and high pH
    • Chizhmakov IV, et al. (2003) Differences in conductance of M2 proton channels of two influenza viruses at low and high pH. J Physiol (London) 546:427-438.
    • (2003) J Physiol (London) , vol.546 , pp. 427-438
    • Chizhmakov, I.V.1
  • 42
    • 0039789834 scopus 로고
    • Elementary steps in enzyme reactions (as studied by relaxation spectrometry)
    • Eigen M, Hammes GG (1963) Elementary steps in enzyme reactions (as studied by relaxation spectrometry). Adv Enzymol Relat Areas Mol Biol 25:1-38.
    • (1963) Adv Enzymol Relat Areas Mol Biol , vol.25 , pp. 1-38
    • Eigen, M.1    Hammes, G.G.2
  • 43
  • 44
    • 1542358793 scopus 로고    scopus 로고
    • De novo folding of membrane proteins: An exploration of the structure and NMR properties of the fd coat protein
    • Im W, Brooks CL, 3rd (2004) De novo folding of membrane proteins: An exploration of the structure and NMR properties of the fd coat protein. J Mol Biol 337:513-519.
    • (2004) J Mol Biol , vol.337 , pp. 513-519
    • Im, W.1    Brooks III, C.L.2
  • 45
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.