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Volumn 9, Issue 5, 2013, Pages

Probing the Energy Landscape of Activation Gating of the Bacterial Potassium Channel KcsA

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; POTASSIUM;

EID: 84878512017     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003058     Document Type: Article
Times cited : (27)

References (66)
  • 1
    • 74549165352 scopus 로고    scopus 로고
    • An introduction to QT interval prolongation and non-clinical approaches to assessing and reducing risk
    • doi: 10.1111/j.1476-5381.2009.00207.x
    • Pollard CE, Abi Gerges N, Bridgland-Taylor MH, Easter A, Hammond TG, et al. (2010) An introduction to QT interval prolongation and non-clinical approaches to assessing and reducing risk. Br J Pharmacol 159: 12-21 doi:10.1111/j.1476-5381.2009.00207.x.
    • (2010) Br J Pharmacol , vol.159 , pp. 12-21
    • Pollard, C.E.1    Abi Gerges, N.2    Bridgland-Taylor, M.H.3    Easter, A.4    Hammond, T.G.5
  • 2
    • 80052338033 scopus 로고    scopus 로고
    • Novel roles for hERG K(+) channels in cell proliferation and apoptosis
    • doi: 10.1038/cddis.2011.77
    • Jehle J, Schweizer PA, Katus HA, Thomas D, (2011) Novel roles for hERG K(+) channels in cell proliferation and apoptosis. Cell Death Dis 2: e193 doi:10.1038/cddis.2011.77.
    • (2011) Cell Death Dis , vol.2
    • Jehle, J.1    Schweizer, P.A.2    Katus, H.A.3    Thomas, D.4
  • 3
    • 33645322386 scopus 로고    scopus 로고
    • KATP channels as molecular sensors of cellular metabolism
    • doi: 10.1038/nature04711
    • Nichols CG, (2006) KATP channels as molecular sensors of cellular metabolism. Nature 440: 470-476 doi:10.1038/nature04711.
    • (2006) Nature , vol.440 , pp. 470-476
    • Nichols, C.G.1
  • 4
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin AL, Huxley AF, (1952) A quantitative description of membrane current and its application to conduction and excitation in nerve. J Physiol 117: 500-544.
    • (1952) J Physiol , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 6
    • 0032478818 scopus 로고    scopus 로고
    • The structure of the potassium channel: molecular basis of K+ conduction and selectivity
    • doi: 10.1126/science.280.5360.69
    • Doyle DA, Morais Cabral J, Pfuetzner RA, Kuo A, Gulbis JM, et al. (1998) The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280: 69-77 doi:10.1126/science.280.5360.69.
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1    Morais Cabral, J.2    Pfuetzner, R.A.3    Kuo, A.4    Gulbis, J.M.5
  • 7
    • 0033516494 scopus 로고    scopus 로고
    • Structural rearrangements underlying K+-channel activation gating
    • doi: 10.1126/science.285.5424.73
    • Perozo E, Cortes DM, Cuello LG, (1999) Structural rearrangements underlying K+-channel activation gating. Science 285: 73-78 doi:10.1126/science.285.5424.73.
    • (1999) Science , vol.285 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 8
    • 0037387189 scopus 로고    scopus 로고
    • Potassium channel gating observed with site-directed mass tagging
    • doi: 10.1038/nsb908
    • Kelly BL, Gross A, (2003) Potassium channel gating observed with site-directed mass tagging. Nat Struct Biol 10: 280-284 doi:10.1038/nsb908.
    • (2003) Nat Struct Biol , vol.10 , pp. 280-284
    • Kelly, B.L.1    Gross, A.2
  • 9
    • 33646145322 scopus 로고    scopus 로고
    • Structural characterization and pH-induced conformational transition of full-length KcsA
    • doi: 10.1529/biophysj.105.071175
    • Zimmer J, Doyle D a, Grossmann JG, (2006) Structural characterization and pH-induced conformational transition of full-length KcsA. Biophys J 90: 1752-1766 doi:10.1529/biophysj.105.071175.
    • (2006) Biophys J , vol.90 , pp. 1752-1766
    • Zimmer, J.1    Doyle, D.2    Grossmann, J.G.3
  • 10
    • 37649021608 scopus 로고    scopus 로고
    • Global twisting motion of single molecular KcsA potassium channel upon gating
    • doi: 10.1016/j.cell.2007.11.040
    • Shimizu H, Iwamoto M, Konno T, Nihei A, Sasaki YC, et al. (2008) Global twisting motion of single molecular KcsA potassium channel upon gating. Cell 132: 67-78 doi:10.1016/j.cell.2007.11.040.
    • (2008) Cell , vol.132 , pp. 67-78
    • Shimizu, H.1    Iwamoto, M.2    Konno, T.3    Nihei, A.4    Sasaki, Y.C.5
  • 11
    • 66149127336 scopus 로고    scopus 로고
    • Crystal structure of full-length KcsA in its closed conformation
    • doi: 10.1073/pnas.0810663106
    • Uysal S, Vásquez V, Tereshko V, Esaki K, Fellouse FA, et al. (2009) Crystal structure of full-length KcsA in its closed conformation. Proc Natl Acad Sci U S A 106: 6644-6649 doi:10.1073/pnas.0810663106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 6644-6649
    • Uysal, S.1    Vásquez, V.2    Tereshko, V.3    Esaki, K.4    Fellouse, F.A.5
  • 12
    • 77954485089 scopus 로고    scopus 로고
    • Structural mechanism of C-type inactivation in K(+) channels
    • doi: 10.1038/nature09153
    • Cuello LG, Jogini V, Cortes DM, Perozo E, (2010) Structural mechanism of C-type inactivation in K(+) channels. Nature 466: 203-208 doi:10.1038/nature09153.
    • (2010) Nature , vol.466 , pp. 203-208
    • Cuello, L.G.1    Jogini, V.2    Cortes, D.M.3    Perozo, E.4
  • 13
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • doi: 10.1038/nature06522
    • Henzler-Wildman K, Kern D, (2007) Dynamic personalities of proteins. Nature 450: 964-972 doi:10.1038/nature06522.
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 14
    • 0036787715 scopus 로고    scopus 로고
    • Open-state models of a potassium channel
    • doi: 10.1016/S0006-3495(02)73951-9
    • Biggin PC, Sansom MSP, (2002) Open-state models of a potassium channel. Biophys J 83: 1867-1876 doi:10.1016/S0006-3495(02)73951-9.
    • (2002) Biophys J , vol.83 , pp. 1867-1876
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 15
    • 4444261061 scopus 로고    scopus 로고
    • In silico activation of KcsA K+ channel by lateral forces applied to the C-termini of inner helices
    • doi: 10.1529/biophysj.103.037770
    • Tikhonov DB, Zhorov BS, (2004) In silico activation of KcsA K+ channel by lateral forces applied to the C-termini of inner helices. Biophys J 87: 1526-1536 doi:10.1529/biophysj.103.037770.
    • (2004) Biophys J , vol.87 , pp. 1526-1536
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 16
    • 23044517429 scopus 로고    scopus 로고
    • Targeted molecular dynamics of an open-state KcsA channel
    • doi: 10.1063/1.1869413
    • Compoint M, Picaud F, Ramseyer C, Girardet C, (2005) Targeted molecular dynamics of an open-state KcsA channel. J Chem Phys 122: 134707 doi:10.1063/1.1869413.
    • (2005) J Chem Phys , vol.122 , pp. 134707
    • Compoint, M.1    Picaud, F.2    Ramseyer, C.3    Girardet, C.4
  • 17
    • 33744926664 scopus 로고    scopus 로고
    • Common mechanism of pore opening shared by five different potassium channels
    • doi: 10.1529/biophysj.105.080093
    • Shrivastava IH, Bahar I, (2006) Common mechanism of pore opening shared by five different potassium channels. Biophys J 90: 3929-3940 doi:10.1529/biophysj.105.080093.
    • (2006) Biophys J , vol.90 , pp. 3929-3940
    • Shrivastava, I.H.1    Bahar, I.2
  • 18
    • 56049102616 scopus 로고    scopus 로고
    • Generation, comparison, and merging of pathways between protein conformations: gating in K-channels
    • doi: 10.1529/biophysj.108.135285
    • Enosh A, Raveh B, Furman-Schueler O, Halperin D, Ben-Tal N, (2008) Generation, comparison, and merging of pathways between protein conformations: gating in K-channels. Biophys J 95: 3850-3860 doi:10.1529/biophysj.108.135285.
    • (2008) Biophys J , vol.95 , pp. 3850-3860
    • Enosh, A.1    Raveh, B.2    Furman-Schueler, O.3    Halperin, D.4    Ben-Tal, N.5
  • 19
    • 50949126927 scopus 로고    scopus 로고
    • Cooperative transition between open and closed conformations in potassium channels
    • doi: 10.1371/journal.pcbi.1000164
    • Haliloglu T, Ben-Tal N, (2008) Cooperative transition between open and closed conformations in potassium channels. PLoS Comput Biol 4: e1000164 doi:10.1371/journal.pcbi.1000164.
    • (2008) PLoS Comput Biol , vol.4
    • Haliloglu, T.1    Ben-Tal, N.2
  • 20
    • 44849124493 scopus 로고    scopus 로고
    • End-point targeted molecular dynamics: large-scale conformational changes in potassium channels
    • doi: 10.1529/biophysj.107.118778
    • Mashl RJ, Jakobsson E, (2008) End-point targeted molecular dynamics: large-scale conformational changes in potassium channels. Biophys J 94: 4307-4319 doi:10.1529/biophysj.107.118778.
    • (2008) Biophys J , vol.94 , pp. 4307-4319
    • Mashl, R.J.1    Jakobsson, E.2
  • 21
    • 77951236840 scopus 로고    scopus 로고
    • Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations
    • doi: 10.1002/prot.22632
    • Denning EJ, Woolf TB, (2010) Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations. Proteins 78: 1105-1119 doi:10.1002/prot.22632.
    • (2010) Proteins , vol.78 , pp. 1105-1119
    • Denning, E.J.1    Woolf, T.B.2
  • 22
    • 36849022651 scopus 로고    scopus 로고
    • Open-state conformation of the KcsA K+ channel: Monte Carlo normal mode following simulations
    • doi: 10.1016/j.str.2007.09.022
    • Miloshevsky G V, Jordan PC, (2007) Open-state conformation of the KcsA K+ channel: Monte Carlo normal mode following simulations. Structure 15: 1654-1662 doi:10.1016/j.str.2007.09.022.
    • (2007) Structure , vol.15 , pp. 1654-1662
    • Miloshevsky, G.V.1    Jordan, P.C.2
  • 23
    • 0029985860 scopus 로고    scopus 로고
    • An efficient method for sampling the essential subspace of proteins
    • doi: 10.1080/07391102.1996.10508874
    • Amadei A, Linssen AB, De Groot BL, Van Aalten DM, Berendsen HJ, (1996) An efficient method for sampling the essential subspace of proteins. J Biomol Struct Dyn 13: 615-625 doi:10.1080/07391102.1996.10508874.
    • (1996) J Biomol Struct Dyn , vol.13 , pp. 615-625
    • Amadei, A.1    Linssen, A.B.2    de Groot, B.L.3    van Aalten, D.M.4    Berendsen, H.J.5
  • 24
    • 0029967692 scopus 로고    scopus 로고
    • Toward an exhaustive sampling of the configurational spaces of the two forms of the peptide hormone guanylin
    • doi: 10.1080/07391102.1996.10508888
    • De Groot BL, Amadei A, Van Aalten DM, Berendsen HJ, (1996) Toward an exhaustive sampling of the configurational spaces of the two forms of the peptide hormone guanylin. J Biomol Struct Dyn 13: 741-751 doi:10.1080/07391102.1996.10508888.
    • (1996) J Biomol Struct Dyn , vol.13 , pp. 741-751
    • de Groot, B.L.1    Amadei, A.2    van Aalten, D.M.3    Berendsen, H.J.4
  • 26
    • 0030833135 scopus 로고    scopus 로고
    • Protein dynamics derived from clusters of crystal structures
    • doi: 10.1016/S0006-3495(97)78317-6
    • Van Aalten DM, Conn DA, De Groot BL, Berendsen HJ, Findlay JB, et al. (1997) Protein dynamics derived from clusters of crystal structures. Biophys J 73: 2891-2896 doi:10.1016/S0006-3495(97)78317-6.
    • (1997) Biophys J , vol.73 , pp. 2891-2896
    • van Aalten, D.M.1    Conn, D.A.2    de Groot, B.L.3    Berendsen, H.J.4    Findlay, J.B.5
  • 27
    • 58149218369 scopus 로고    scopus 로고
    • Protein Folding Pathways Revealed by Essential Dynamics Sampling
    • doi: 10.1021/ct800157v
    • Narzi D, Daidone I, Amadei A, Di Nola A, (2008) Protein Folding Pathways Revealed by Essential Dynamics Sampling. J Chem Theory Comput 4: 1940-1948 doi:10.1021/ct800157v.
    • (2008) J Chem Theory Comput , vol.4 , pp. 1940-1948
    • Narzi, D.1    Daidone, I.2    Amadei, A.3    Di Nola, A.4
  • 28
    • 77949325249 scopus 로고    scopus 로고
    • Symmetry-restrained molecular dynamics simulations improve homology models of potassium channels
    • doi: 10.1002/prot.22618
    • Anishkin A, Milac AL, Guy HR, (2010) Symmetry-restrained molecular dynamics simulations improve homology models of potassium channels. Proteins 78: 932-949 doi:10.1002/prot.22618.
    • (2010) Proteins , vol.78 , pp. 932-949
    • Anishkin, A.1    Milac, A.L.2    Guy, H.R.3
  • 29
    • 0042213113 scopus 로고    scopus 로고
    • Molecular dynamics of the KcsA K(+) channel in a bilayer membrane
    • doi: 10.1016/S0006-3495(00)76831-7
    • Bernèche S, Roux B, (2000) Molecular dynamics of the KcsA K(+) channel in a bilayer membrane. Biophys J 78: 2900-2917 doi:10.1016/S0006-3495(00)76831-7.
    • (2000) Biophys J , vol.78 , pp. 2900-2917
    • Bernèche, S.1    Roux, B.2
  • 30
    • 33748802222 scopus 로고    scopus 로고
    • Surface structure and its dynamic rearrangements of the KcsA potassium channel upon gating and tetrabutylammonium blocking
    • doi: 10.1074/jbc.M602018200
    • Iwamoto M, Shimizu H, Inoue F, Konno T, Sasaki YC, et al. (2006) Surface structure and its dynamic rearrangements of the KcsA potassium channel upon gating and tetrabutylammonium blocking. J Biol Chem 281: 28379-28386 doi:10.1074/jbc.M602018200.
    • (2006) J Biol Chem , vol.281 , pp. 28379-28386
    • Iwamoto, M.1    Shimizu, H.2    Inoue, F.3    Konno, T.4    Sasaki, Y.C.5
  • 31
    • 84872189670 scopus 로고    scopus 로고
    • Amphipathic antenna of an inward rectifier K+ channel responds to changes in the inner membrane leaflet
    • doi: 10.1073/pnas.1217323110
    • Iwamoto M, Oiki S, (2013) Amphipathic antenna of an inward rectifier K+ channel responds to changes in the inner membrane leaflet. Proc Natl Acad Sci U S A 110: 749-754 doi:10.1073/pnas.1217323110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 749-754
    • Iwamoto, M.1    Oiki, S.2
  • 32
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • doi: 10.1016/S0263-7855(97)00009-X
    • Smart OS, Neduvelil JG, Wang X, Wallace BA, Sansom MSP, (1996) HOLE: A program for the analysis of the pore dimensions of ion channel structural models. J Mol Graph 14: 354-360 doi:10.1016/S0263-7855(97)00009-X.
    • (1996) J Mol Graph , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.P.5
  • 33
    • 77954515664 scopus 로고    scopus 로고
    • Structural basis for the coupling between activation and inactivation gates in K(+) channels
    • doi: 10.1038/nature09136
    • Cuello LG, Jogini V, Cortes DM, Pan AC, Gagnon DG, et al. (2010) Structural basis for the coupling between activation and inactivation gates in K(+) channels. Nature 466: 272-275 doi:10.1038/nature09136.
    • (2010) Nature , vol.466 , pp. 272-275
    • Cuello, L.G.1    Jogini, V.2    Cortes, D.M.3    Pan, A.C.4    Gagnon, D.G.5
  • 34
    • 84855505933 scopus 로고    scopus 로고
    • Thermodynamic coupling between activation and inactivation gating in potassium channels revealed by free energy molecular dynamics simulations
    • doi: 10.1085/jgp.201110670
    • Pan AC, Cuello LG, Perozo E, Roux B, (2011) Thermodynamic coupling between activation and inactivation gating in potassium channels revealed by free energy molecular dynamics simulations. J Gen Physiol 138: 571-580 doi:10.1085/jgp.201110670.
    • (2011) J Gen Physiol , vol.138 , pp. 571-580
    • Pan, A.C.1    Cuello, L.G.2    Perozo, E.3    Roux, B.4
  • 35
    • 33745041507 scopus 로고    scopus 로고
    • Molecular determinants of gating at the potassium-channel selectivity filter
    • doi: 10.1038/nsmb1069
    • Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, et al. (2006) Molecular determinants of gating at the potassium-channel selectivity filter. Nat Struct Mol Biol 13: 311-318 doi:10.1038/nsmb1069.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 311-318
    • Cordero-Morales, J.F.1    Cuello, L.G.2    Zhao, Y.3    Jogini, V.4    Cortes, D.M.5
  • 36
    • 35848958366 scopus 로고    scopus 로고
    • Molecular driving forces determining potassium channel slow inactivation
    • doi: 10.1038/nsmb1309
    • Cordero-Morales JF, Jogini V, Lewis A, Vásquez V, Cortes DM, et al. (2007) Molecular driving forces determining potassium channel slow inactivation. Nat Struct Mol Biol 14: 1062-1069 doi:10.1038/nsmb1309.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1062-1069
    • Cordero-Morales, J.F.1    Jogini, V.2    Lewis, A.3    Vásquez, V.4    Cortes, D.M.5
  • 37
    • 84866560561 scopus 로고    scopus 로고
    • Protonation state of E71 in KcsA and its role for channel collapse and inactivation
    • doi: 10.1073/pnas.1211900109
    • Bhate MP, McDermott AE, (2012) Protonation state of E71 in KcsA and its role for channel collapse and inactivation. Proc Natl Acad Sci U S A 2012: 1-6 doi:10.1073/pnas.1211900109.
    • (2012) Proc Natl Acad Sci U S A , vol.2012 , pp. 1-6
    • Bhate, M.P.1    McDermott, A.E.2
  • 38
    • 0034690250 scopus 로고    scopus 로고
    • Ion permeation mechanism of the potassium channel
    • doi: 10.1038/35009114
    • Aqvist J, Luzhkov V, (2000) Ion permeation mechanism of the potassium channel. Nature 404: 881-884 doi:10.1038/35009114.
    • (2000) Nature , vol.404 , pp. 881-884
    • Aqvist, J.1    Luzhkov, V.2
  • 39
    • 0037137218 scopus 로고    scopus 로고
    • Opening the KcsA K + Channel: Tryptophan Scanning and Complementation Analysis Lead to Mutants with Altered Gating
    • doi: 10.1021/bi026393r
    • Irizarry SN, Kutluay E, Drews G, Hart SJ, Heginbotham L, (2002) Opening the KcsA K + Channel: Tryptophan Scanning and Complementation Analysis Lead to Mutants with Altered Gating. Biochemistry 41: 13653-13662 doi:10.1021/bi026393r.
    • (2002) Biochemistry , vol.41 , pp. 13653-13662
    • Irizarry, S.N.1    Kutluay, E.2    Drews, G.3    Hart, S.J.4    Heginbotham, L.5
  • 40
    • 0037131520 scopus 로고    scopus 로고
    • Energetics of Pore Opening in a Voltage-Gated K+ Channel
    • doi: 10.1016/S0092-8674(02)01013-9
    • Yifrach O, MacKinnon R, (2002) Energetics of Pore Opening in a Voltage-Gated K+ Channel. Cell 111: 231-239 doi:10.1016/S0092-8674(02)01013-9.
    • (2002) Cell , vol.111 , pp. 231-239
    • Yifrach, O.1    MacKinnon, R.2
  • 41
    • 38049148291 scopus 로고    scopus 로고
    • Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel
    • doi: 10.1073/pnas.0708120104
    • Sadovsky E, Yifrach O, (2007) Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel. Proc Natl Acad Sci U S A 104: 19813-19818 doi:10.1073/pnas.0708120104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19813-19818
    • Sadovsky, E.1    Yifrach, O.2
  • 42
    • 64149115115 scopus 로고    scopus 로고
    • Genetic selection of activatory mutations in KcsA
    • doi: 10.4161/chan.2.6.6874
    • Paynter J, Sarkies P, Andres-Enguix I, Tucker SJ, (2008) Genetic selection of activatory mutations in KcsA. Channels 2: 413-418 doi:10.4161/chan.2.6.6874.
    • (2008) Channels , vol.2 , pp. 413-418
    • Paynter, J.1    Sarkies, P.2    Andres-Enguix, I.3    Tucker, S.J.4
  • 43
    • 66149157329 scopus 로고    scopus 로고
    • Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels
    • doi: 10.1371/journal.pbio.1000047
    • Lee S-Y, Banerjee A, MacKinnon R, (2009) Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels. PLoS Biol 7: e47 doi:10.1371/journal.pbio.1000047.
    • (2009) PLoS Biol , vol.7
    • Lee, S.-Y.1    Banerjee, A.2    MacKinnon, R.3
  • 44
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K+ channel
    • doi: 10.1038/nature01580
    • Jiang Y, Lee A, Chen J, Ruta V, Cadene M, et al. (2003) X-ray structure of a voltage-dependent K+ channel. Nature 423: 33-41 doi:10.1038/nature01580.
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Ruta, V.4    Cadene, M.5
  • 45
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • doi: 10.1126/science.1116269
    • Long SB, Campbell EB, Mackinnon R, (2005) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309: 897-903 doi:10.1126/science.1116269.
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 46
    • 0036016539 scopus 로고    scopus 로고
    • Scanning the Intracellular S6 Activation Gate in the Shaker K+ Channel
    • doi: 10.1085/jgp.20028569
    • Hackos DH, (2002) Scanning the Intracellular S6 Activation Gate in the Shaker K+ Channel. J Gen Physiol 119: 521-532 doi:10.1085/jgp.20028569.
    • (2002) J Gen Physiol , vol.119 , pp. 521-532
    • Hackos, D.H.1
  • 47
    • 0033761957 scopus 로고    scopus 로고
    • A Localized Interaction Surface for Voltage-Sensing Domains on the Pore Domain of a K+ Channel
    • doi: 10.1016/S0896-6273(00)80904-6
    • Li-Smerin Y, Hackos DH, Swartz KJ, (2000) A Localized Interaction Surface for Voltage-Sensing Domains on the Pore Domain of a K+ Channel. Neuron 25: 411-423 doi:10.1016/S0896-6273(00)80904-6.
    • (2000) Neuron , vol.25 , pp. 411-423
    • Li-Smerin, Y.1    Hackos, D.H.2    Swartz, K.J.3
  • 48
    • 0026663246 scopus 로고
    • Evidence for cooperative interactions in potassium channel gating
    • doi: 10.1038/359420a0
    • Tytgat J, Hess P, (1992) Evidence for cooperative interactions in potassium channel gating. Nature 359: 420-423 doi:10.1038/359420a0.
    • (1992) Nature , vol.359 , pp. 420-423
    • Tytgat, J.1    Hess, P.2
  • 49
    • 0031905513 scopus 로고    scopus 로고
    • Role of the S4 in cooperativity of voltage-dependent potassium channel activation
    • doi: 10.1085/jgp.111.3.399
    • Smith-Maxwell CJ, Ledwell JL, Aldrich RW, (1998) Role of the S4 in cooperativity of voltage-dependent potassium channel activation. J Gen Physiol 111: 399-420 doi:10.1085/jgp.111.3.399.
    • (1998) J Gen Physiol , vol.111 , pp. 399-420
    • Smith-Maxwell, C.J.1    Ledwell, J.L.2    Aldrich, R.W.3
  • 50
    • 0032894433 scopus 로고    scopus 로고
    • Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation
    • doi: 10.1085/jgp.113.3.389
    • Ledwell JL, Aldrich RW, (1999) Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation. J Gen Physiol 113: 389-414 doi:10.1085/jgp.113.3.389.
    • (1999) J Gen Physiol , vol.113 , pp. 389-414
    • Ledwell, J.L.1    Aldrich, R.W.2
  • 51
    • 12344259926 scopus 로고    scopus 로고
    • The cooperative voltage sensor motion that gates a potassium channel
    • doi: 10.1085/jgp.200409197
    • Pathak M, Kurtz L, Tombola F, Isacoff E, (2005) The cooperative voltage sensor motion that gates a potassium channel. J Gen Physiol 125: 57-69 doi:10.1085/jgp.200409197.
    • (2005) J Gen Physiol , vol.125 , pp. 57-69
    • Pathak, M.1    Kurtz, L.2    Tombola, F.3    Isacoff, E.4
  • 52
    • 58149527755 scopus 로고    scopus 로고
    • Fluorescence detection of the movement of single KcsA subunits reveals cooperativity
    • doi: 10.1073/pnas.0807056106
    • Blunck R, McGuire H, Hyde HC, Bezanilla F, (2008) Fluorescence detection of the movement of single KcsA subunits reveals cooperativity. Proc Natl Acad Sci U S A 105: 20263-20268 doi:10.1073/pnas.0807056106.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20263-20268
    • Blunck, R.1    McGuire, H.2    Hyde, H.C.3    Bezanilla, F.4
  • 53
    • 50149112602 scopus 로고    scopus 로고
    • Direct analysis of cooperativity in multisubunit allosteric proteins
    • doi: 10.1073/pnas.0804104105
    • Zandany N, Ovadia M, Orr I, Yifrach O, (2008) Direct analysis of cooperativity in multisubunit allosteric proteins. Proc Natl Acad Sci U S A 105: 11697-11702 doi:10.1073/pnas.0804104105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11697-11702
    • Zandany, N.1    Ovadia, M.2    Orr, I.3    Yifrach, O.4
  • 54
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution
    • doi: 10.1038/35102009
    • Zhou Y, Morais-Cabral JH, Kaufman A, MacKinnon R, (2001) Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature 414: 43-48 doi:10.1038/35102009.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 55
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • doi: 10.1002/elps.1150181505
    • Guex N, Peitsch MC, (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723 doi:10.1002/elps.1150181505.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 56
    • 77954256616 scopus 로고    scopus 로고
    • g_membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • doi: 10.1002/jcc.21507
    • Wolf MG, Hoefling M, Aponte-Santamaría C, Grubmüller H, Groenhof G, (2010) g_membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation. J Comput Chem 31: 2169-2174 doi:10.1002/jcc.21507.
    • (2010) J Comput Chem , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamaría, C.3    Grubmüller, H.4    Groenhof, G.5
  • 57
    • 83455205897 scopus 로고    scopus 로고
    • In silico Analysis of Conformational Changes Induced by Mutation of Aromatic Binding Residues: Consequences for Drug Binding in the hERG K+ Channel
    • doi: 10.1371/journal.pone.0028778
    • Knape K, Linder T, Wolschann P, Beyer A, Stary-Weinzinger A, (2011) In silico Analysis of Conformational Changes Induced by Mutation of Aromatic Binding Residues: Consequences for Drug Binding in the hERG K+ Channel. PloS one 6: e28778 doi:10.1371/journal.pone.0028778.
    • (2011) PloS One , vol.6
    • Knape, K.1    Linder, T.2    Wolschann, P.3    Beyer, A.4    Stary-Weinzinger, A.5
  • 58
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • doi: 10.1021/ct700301q
    • Hess B, Kutzner C, Van der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput 4: 435-447 doi:10.1021/ct700301q.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 59
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • doi: 10.1002/prot.21123
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, et al. (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65: 712-725 doi:10.1002/prot.21123.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5
  • 60
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • doi: 10.1063/1.445869
    • Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML, (1983) Comparison of simple potential functions for simulating liquid water. J Chem Phys 79: 926 doi:10.1063/1.445869.
    • (1983) J Chem Phys , vol.79 , pp. 926
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 61
    • 41549149586 scopus 로고    scopus 로고
    • Biomolecular simulations of membranes: physical properties from different force fields
    • doi: 10.1063/1.2897760
    • Siu SWI, Vácha R, Jungwirth P, Böckmann R a, (2008) Biomolecular simulations of membranes: physical properties from different force fields. J Chem Phys 128: 125103 doi:10.1063/1.2897760.
    • (2008) J Chem Phys , vol.128 , pp. 125103
    • Siu, S.W.I.1    Vácha, R.2    Jungwirth, P.3    Böckmann, R.4
  • 62
    • 37649031391 scopus 로고    scopus 로고
    • Diffuse scattering provides material parameters and electron density profiles of biomembranes
    • doi: 10.1103/PhysRevE.69.040901
    • Liu Y, Nagle JF, (2004) Diffuse scattering provides material parameters and electron density profiles of biomembranes. Phys Rev E: Stat, Nonlinear, Soft Matter Phys 69: 040901 doi:10.1103/PhysRevE.69.040901.
    • (2004) Phys Rev E: Stat, Nonlinear, Soft Matter Phys , vol.69 , pp. 040901
    • Liu, Y.1    Nagle, J.F.2
  • 63
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • doi: 10.1063/1.464397
    • Darden T, York D, Pedersen L, (1993) Particle mesh Ewald: An N log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089 doi:10.1063/1.464397.
    • (1993) J Chem Phys , vol.98 , pp. 10089
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 65
    • 0027441950 scopus 로고
    • Essential dynamics of proteins
    • doi: 10.1002/prot.340170408
    • Amadei A, Linssen AB, Berendsen HJ, (1993) Essential dynamics of proteins. Proteins 17: 412-425 doi:10.1002/prot.340170408.
    • (1993) Proteins , vol.17 , pp. 412-425
    • Amadei, A.1    Linssen, A.B.2    Berendsen, H.J.3
  • 66
    • 78651282170 scopus 로고    scopus 로고
    • g_wham-A Free Weighted Histogram Analysis Implementation Including Robust Error and Autocorrelation Estimates
    • doi: 10.1021/ct100494z
    • Hub JS, De Groot BL, Van der Spoel D, (2010) g_wham-A Free Weighted Histogram Analysis Implementation Including Robust Error and Autocorrelation Estimates. J Chem Theory Comput 6: 3713-3720 doi:10.1021/ct100494z.
    • (2010) J Chem Theory Comput , vol.6 , pp. 3713-3720
    • Hub, J.S.1    de Groot, B.L.2    van der Spoel, D.3


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