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Volumn 26, Issue 8, 2009, Pages 397-421

From the gating charge response to pore domain movement: Initial motions of Kv1.2 dynamics under physiological voltage changes

Author keywords

Double layer effect; Ionic solution; S4 domain; Voltage gating

Indexed keywords

POTASSIUM CHANNEL KV1.2;

EID: 70350787095     PISSN: 09687688     EISSN: 14645203     Source Type: Journal    
DOI: 10.3109/09687680903278539     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 41149095488 scopus 로고    scopus 로고
    • How membrane proteins sense voltage
    • Bezanilla F. 2008. How membrane proteins sense voltage. Nat Rev Mol Cell Biol. 9:323-332.
    • (2008) Nat Rev Mol Cell Biol. , vol.9 , pp. 323-332
    • Bezanilla, F.1
  • 3
    • 49549083949 scopus 로고    scopus 로고
    • Membrane proteins: Molecular dynamics simulations
    • Lindahl E, Sansom MSP. 2008. Membrane proteins: Molecular dynamics simulations. Curr Opinion Struct Biol. 18:425-431.
    • (2008) Curr Opinion Struct Biol. , vol.18 , pp. 425-431
    • Lindahl, E.1    Sansom, M.S.P.2
  • 4
    • 33751249039 scopus 로고    scopus 로고
    • Dissecting the coupling between the voltage sensor and pore domains
    • Roux B. 2007. Dissecting the coupling between the voltage sensor and pore domains. Neuron. 52:568-569.
    • (2007) Neuron. , vol.52 , pp. 568-569
    • Roux, B.1
  • 5
    • 36048967024 scopus 로고    scopus 로고
    • The last few frames of the voltage-gating movie
    • Sigworth FJ. 2007. The last few frames of the voltage-gating movie. Biophys J. 93:2981-2983.
    • (2007) Biophys J. , vol.93 , pp. 2981-2983
    • Sigworth, F.J.1
  • 6
    • 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
  • 8
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long SB, Campbell EB, MacKinnon R. 2005. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel Science. 309:897-903.
    • (2005) Science. , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 9
    • 58149162833 scopus 로고    scopus 로고
    • The membrane potential and its representation by a constant electric field in computer simulations
    • Roux B. 2008. The membrane potential and its representation by a constant electric field in computer simulations. Biophys J. 95:4205-4216.
    • (2008) Biophys J. , vol.95 , pp. 4205-4216
    • Roux, B.1
  • 10
    • 43949121752 scopus 로고    scopus 로고
    • Modeling membranes under a transmembrane potential
    • Delemotte L, Dehez F, Treptow W, TarekM. 2008. Modeling membranes under a transmembrane potential. J Phys Chem D. 112:5547-5550.
    • (2008) J Phys Chem D. , vol.112 , pp. 5547-5550
    • Delemotte, L.1    Dehez, F.2    Treptow, W.3    Tarek, M.4
  • 11
    • 34547628129 scopus 로고    scopus 로고
    • + channel in a membrane environment
    • DOI 10.1529/biophysj.107.112540
    • Jogini V, Roux B. 2007. Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Biophys J. 93:3070-3082. (Pubitemid 350097098)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 3070-3082
    • Jogini, V.1    Roux, B.2
  • 12
    • 43649093151 scopus 로고    scopus 로고
    • Molecular dynamics simulations of asymmetric NaCl and KCl solutions separated by phosphatidylcholine bilayers: Potential drops and structural changes induced by strong Na+-lipid interactions and finite size effects
    • Lee S-J, Song Y, Baker NA. 2008. Molecular dynamics simulations of asymmetric NaCl and KCl solutions separated by phosphatidylcholine bilayers: Potential drops and structural changes induced by strong Na+-lipid interactions and finite size effects. Biophys J. 94:3565-3576.
    • (2008) Biophys J. , vol.94 , pp. 3565-3576
    • Lee, S.-J.1    Song, Y.2    Baker, N.A.3
  • 13
    • 11144342719 scopus 로고    scopus 로고
    • Atomistic simulations of biologically realistic transmembrane potential gradients
    • Sachs JN, Crozier PS, Woolf TB. 2004. Atomistic simulations of biologically realistic transmembrane potential gradients. J Chem Phys. 121:10847-10851.
    • (2004) J Chem Phys. , vol.121 , pp. 10847-10851
    • Sachs, J.N.1    Crozier, P.S.2    Woolf, T.B.3
  • 14
    • 55949123442 scopus 로고    scopus 로고
    • Double bilayers and transmembrane gradients: A molecular dynamics study of a highly charged peptide
    • Denning EJ, Woolf TB. 2008. Double bilayers and transmembrane gradients: A molecular dynamics study of a highly charged peptide. Biophys J. 95:3161-3173.
    • (2008) Biophys J. , vol.95 , pp. 3161-3173
    • Denning, E.J.1    Woolf, T.B.2
  • 19
    • 0842333152 scopus 로고    scopus 로고
    • Implicit solvation based on generalized Born theory in different dielectric environments
    • Feig M, Im W, Brooks CL. 2004. Implicit solvation based on generalized Born theory in different dielectric environments. J Chem Phys. 120:903-911.
    • (2004) J Chem Phys. , vol.120 , pp. 903-911
    • Feig, M.1    Im, W.2    Brooks, C.L.3
  • 20
    • 0346971105 scopus 로고    scopus 로고
    • Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures
    • Feig M, Onufriev A, Lee MS, Im W, Case DA, Brooks CL. 2004. Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures. J Comp Chem. 25:265-284.
    • (2004) J Comp Chem. , vol.25 , pp. 265-284
    • Feig, M.1    Onufriev, A.2    Lee, M.S.3    Im, W.4    Case, D.A.5    Brooks, C.L.6
  • 21
    • 0242322528 scopus 로고    scopus 로고
    • An Implicit Membrane Generalized Born Theory for the Study of Structure, Stability, and Interactions of Membrane Proteins
    • Im W, Feig M, Brooks CL III. 2003. An implicit membrane generalized Born theory for the study of structure, stability, and interactions of membrane proteins. Biophys J. 85:2900-2918. (Pubitemid 37345782)
    • (2003) Biophysical Journal , vol.85 , Issue.5 , pp. 2900-2918
    • Im, W.1    Feig, M.2    Brooks III, C.L.3
  • 22
    • 0141956090 scopus 로고    scopus 로고
    • Generalized Born model with a simple smoothing function
    • Im W, Lee MS, Brooks CL III. 2003. Generalized Born model with a simple smoothing function. J Comp Chem. 24:1691-1702.
    • (2003) J Comp Chem. , vol.24 , pp. 1691-1702
    • Im, W.1    Lee, M.S.2    Brooks III, C.L.3
  • 23
    • 0002467378 scopus 로고
    • Fast parallel algorithms for short-range molecular dynamics
    • Plimpton SJ. 1995. Fast parallel algorithms for short-range molecular dynamics. J Comp Phys. 117:1-19.
    • (1995) J Comp Phys. , vol.117 , pp. 1-19
    • Plimpton, S.J.1
  • 25
    • 70350746893 scopus 로고    scopus 로고
    • Accessed from the website
    • Michaud-Agrawal N. Accessed from the website: http://code. google. com/p/mdanalysis.
    • Michaud-Agrawal, N.1
  • 27
    • 33646135082 scopus 로고    scopus 로고
    • Environment of the gating charges in the Kv 1.2 Shaker Potassium Channel
    • Treptow W, Tarek M. 2006. Environment of the gating charges in the Kv 1.2 Shaker Potassium Channel. Biophys J. 90:L64-66.
    • (2006) Biophys J. , vol.90
    • Treptow, W.1    Tarek, M.2
  • 28
    • 33846785439 scopus 로고    scopus 로고
    • How Does a Voltage Sensor Interact with a Lipid Bilayer? Simulations of a Potassium Channel Domain
    • DOI 10.1016/j.str.2007.01.004, PII S0969212607000330
    • Sands Z, Sansom MSP. 2007. How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain. Structure. 15:235-244. (Pubitemid 46209817)
    • (2007) Structure , vol.15 , Issue.2 , pp. 235-244
    • Sands, Z.A.1    Sansom, M.S.P.2
  • 29
    • 42649130377 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the Escherichia coli NikR protein: Equilibrium conformational fluctuations reveal interdomain allosteric communication pathways
    • Bradley MJ, Chivers PT, Baker NA. 2008. Molecular dynamics simulation of the Escherichia coli NikR protein: Equilibrium conformational fluctuations reveal interdomain allosteric communication pathways. J Molec Biol. 378:1155-1173.
    • (2008) J Molec Biol. , vol.378 , pp. 1155-1173
    • Bradley, M.J.1    Chivers, P.T.2    Baker, N.A.3
  • 30
    • 50349088433 scopus 로고    scopus 로고
    • Molecular dynamics simulation of Kv channel voltage sensor helix in a lipid membrane with applied electric field
    • Nishizawa M, Nishizawa K. 2008. Molecular dynamics simulation of Kv channel voltage sensor helix in a lipid membrane with applied electric field. Biophysical J. 95:1729-1744.
    • (2008) Biophysical J. , vol.95 , pp. 1729-1744
    • Nishizawa, M.1    Nishizawa, K.2
  • 31
    • 25644437209 scopus 로고    scopus 로고
    • Focused electric field across the voltage sensor of potassium channels
    • DOI 10.1016/j.neuron.2005.08.020, PII S0896627305006951
    • Ahem C, Horn R. 2005. Focused electric field across the voltage sensor of potassium channels. Neuron. 48:25-29. (Pubitemid 41384163)
    • (2005) Neuron , vol.48 , Issue.1 , pp. 25-29
    • Ahern, C.A.1    Horn, R.2
  • 33
    • 34247626293 scopus 로고    scopus 로고
    • Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment
    • DOI 10.1085/jgp.200709745
    • MacCallum J, Bennett WFD, Tieleman DP. 2007. Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment. J Gen Physiol. 129:371-377. (Pubitemid 46686453)
    • (2007) Journal of General Physiology , vol.129 , Issue.5 , pp. 371-377
    • MacCallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 34
    • 50549085702 scopus 로고    scopus 로고
    • Potential of mean force and pKa profile calculation for a lipid membrane-exposed arginine side chain
    • Li L, Vorobyov I, Allen TW. 2008. Potential of mean force and pKa profile calculation for a lipid membrane-exposed arginine side chain. J Phys Chem B. 112:9574-9587.
    • (2008) J Phys Chem B. , vol.112 , pp. 9574-9587
    • Li, L.1    Vorobyov, I.2    Allen, T.W.3
  • 35
    • 41449090448 scopus 로고    scopus 로고
    • Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening
    • Marius P, Zagnoni M, Sandison ME, East JM, Morgan H, Lee AG. 2008. Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening. Biophys J. 94:1689-1698.
    • (2008) Biophys J. , vol.94 , pp. 1689-1698
    • Marius, P.1    Zagnoni, M.2    Sandison, M.E.3    East, J.M.4    Morgan, H.5    Lee, A.G.6
  • 36
    • 0036789731 scopus 로고    scopus 로고
    • Interactions of phospholipids with the potassium channel KcsA
    • Williamson IM, Alvis SJ, East JM, Lee AG. 2002. Interactions of phospholipids with the potassium channel KcsA. Biophys J. 83:2026-2038.
    • (2002) Biophys J. , vol.83 , pp. 2026-2038
    • Williamson, I.M.1    Alvis, S.J.2    East, J.M.3    Lee, A.G.4
  • 37
    • 39149109885 scopus 로고    scopus 로고
    • + channels
    • DOI 10.1038/nature06618, PII NATURE06618
    • Xu Y, Ramu Y, Lu Z. 2008. Removal of phospho-head groups of membrane lipids immobilizes voltage sensors of K+ channel. Nature. 451:826-829. (Pubitemid 351253175)
    • (2008) Nature , vol.451 , Issue.7180 , pp. 826-829
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 38
    • 5644258235 scopus 로고    scopus 로고
    • + channel in a lipid bilayer
    • DOI 10.1126/science.1101373
    • Cuello LG, Cortes DM, Perozo E. 2004. Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer. Science. 306:491-495. (Pubitemid 39372450)
    • (2004) Science , vol.306 , Issue.5695 , pp. 491-495
    • Cuello, L.G.1    Cortes, D.M.2    Perozo, E.3
  • 40
    • 23844459909 scopus 로고    scopus 로고
    • Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement
    • DOI 10.1038/nature03888
    • Chanda B, Asamoah OK, Blunck R, Roux B, Bezanilla F. 2005. Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement. Nature. 436:852-856. (Pubitemid 41160644)
    • (2005) Nature , vol.436 , Issue.7052 , pp. 852-856
    • Chanda, B.1    Asamoah, O.K.2    Blunck, R.3    Roux, B.4    Bezanilla, F.5
  • 41
    • 27244444569 scopus 로고    scopus 로고
    • Interface connections of a transmembrane voltage sensor
    • Freites JA, Tobias DJ, von Heijne G, White SH. 2005. Interface connections of a transmembrane voltage sensor. PNAS. 102:15059-15064.
    • (2005) PNAS. , vol.102 , pp. 15059-15064
    • Freites, J.A.1    Tobias, D.J.2    Von Heijne, G.3    White, S.H.4
  • 44
    • 61449172924 scopus 로고    scopus 로고
    • Conformational changes and slow dynamics through microsecond polarized atomistic molecular simulation of an integral Kv1.2 ion channel
    • Bjelkmar P, Niemelä PS, Vattulainen L, Lindahl E. 2009. Conformational changes and slow dynamics through microsecond polarized atomistic molecular simulation of an integral Kv1.2 ion channel. PLoS Computational Biol. 5:c1000289.
    • (2009) PLoS Computational Biol. , vol.5
    • Bjelkmar, P.1    Niemelä, P.S.2    Vattulainen, L.3    Lindahl, E.4
  • 45
    • 45949109759 scopus 로고    scopus 로고
    • Gating motions in voltage-gated potassium channels revealed by coarse-grained molecular dynamics simulations
    • Treptow W, Marrink SJ, Tarek M. 2008. Gating motions in voltage-gated potassium channels revealed by coarse-grained molecular dynamics simulations. J Phys Chem B Lett. 112:3277-3282.
    • (2008) J Phys Chem B Lett. , vol.112 , pp. 3277-3282
    • Treptow, W.1    Marrink, S.J.2    Tarek, M.3
  • 46
    • 59649096789 scopus 로고    scopus 로고
    • Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by noninteracting residues
    • Labro AJ, Raes, AL, Grottesi G, Hoorick D, Sansom MSP, Snyders DJ. 2008. Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by noninteracting residues. J Gen Physiol. 132:667-680.
    • (2008) J Gen Physiol. , vol.132 , pp. 667-680
    • Labro, A.J.1    Raes, A.L.2    Grottesi, G.3    Hoorick, D.4    Sansom, M.S.P.5    Snyders, D.J.6
  • 47
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • DOI 10.1038/nature06265, PII NATURE06265
    • Long SB, Tao X, Campbell EB, MacKinnon R. 2007. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature. 450:376-382. (Pubitemid 350126743)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4


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