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Volumn 124, Issue 3, 2006, Pages 279-291

Ion selectivity in potassium channels

Author keywords

Hydration; Membrane; Molecular dynamics; Potassium; Proteins; Sodium; Solvation

Indexed keywords

CARBONYL DERIVATIVE; CATION; LIGAND; POTASSIUM CHANNEL; POTASSIUM ION; SODIUM ION; THREONINE; VALINOMYCIN;

EID: 33750609826     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.05.033     Document Type: Article
Times cited : (173)

References (80)
  • 5
    • 0142185496 scopus 로고    scopus 로고
    • + selectivity filter: charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates
    • + selectivity filter: charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates. J. Mol. Biol. 333 (2003) 965-975
    • (2003) J. Mol. Biol. , vol.333 , pp. 965-975
    • Zhou, Y.1    MacKinnon, R.2
  • 6
    • 0032853087 scopus 로고    scopus 로고
    • Ion channels: from idea to reality
    • Hille B., Armstrong C.M., and MacKinnon R. Ion channels: from idea to reality. Nat. Med. 5 (1999) 1105-1109
    • (1999) Nat. Med. , vol.5 , pp. 1105-1109
    • Hille, B.1    Armstrong, C.M.2    MacKinnon, R.3
  • 7
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen G. The voltage-gated potassium channels and their relatives. Nature 419 (2002) 35-42
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 8
    • 0038487878 scopus 로고    scopus 로고
    • Voltage-gated K channels
    • Armstrong C. Voltage-gated K channels. Sci. STKE 188 (2003) re10
    • (2003) Sci. STKE , vol.188
    • Armstrong, C.1
  • 9
    • 0038298804 scopus 로고    scopus 로고
    • Modeling permeation energetics in the KcsA potassium channel
    • Garofoli S., and Jordan P.C. Modeling permeation energetics in the KcsA potassium channel. Biophys. J. 84 (2003) 2814-2830
    • (2003) Biophys. J. , vol.84 , pp. 2814-2830
    • Garofoli, S.1    Jordan, P.C.2
  • 13
    • 70449252824 scopus 로고
    • The penetration of some cation into muscle
    • Mullins L.J. The penetration of some cation into muscle. J. Gen. Physiol. 42 (1959) 817-829
    • (1959) J. Gen. Physiol. , vol.42 , pp. 817-829
    • Mullins, L.J.1
  • 14
    • 33750611185 scopus 로고
    • Negative conductance caused by entry of sodium and cesium ions into the K channels of squid axon
    • Bezanilla F., and Armstrong C.M. Negative conductance caused by entry of sodium and cesium ions into the K channels of squid axon. J. Gen. Physiol. 53 (1972) 342-347
    • (1972) J. Gen. Physiol. , vol.53 , pp. 342-347
    • Bezanilla, F.1    Armstrong, C.M.2
  • 16
    • 0015881172 scopus 로고
    • Potassium channels in myelinated nerve-selective permeability to small cations
    • Hille B. Potassium channels in myelinated nerve-selective permeability to small cations. J. Gen. Physiol. 61 (1973) 599
    • (1973) J. Gen. Physiol. , vol.61 , pp. 599
    • Hille, B.1
  • 17
    • 73049154846 scopus 로고
    • Cation selective electrodes and their mode of operation
    • Eisenman G. Cation selective electrodes and their mode of operation. Biophys. J. 2 (1962) 259-323
    • (1962) Biophys. J. , vol.2 , pp. 259-323
    • Eisenman, G.1
  • 19
    • 29244449328 scopus 로고    scopus 로고
    • Three computational methods for studying permeation, selectivity and dynamics in biological ion channels
    • Chung S.H., and Corry B. Three computational methods for studying permeation, selectivity and dynamics in biological ion channels. Soft Mater. 1 (2005) 417-427
    • (2005) Soft Mater. , vol.1 , pp. 417-427
    • Chung, S.H.1    Corry, B.2
  • 20
    • 7244251461 scopus 로고    scopus 로고
    • Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands
    • Noskov S.Y., Berneche S., and Roux B. Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands. Nature 431 (2004) 830-834
    • (2004) Nature , vol.431 , pp. 830-834
    • Noskov, S.Y.1    Berneche, S.2    Roux, B.3
  • 21
    • 0037071785 scopus 로고    scopus 로고
    • Potassium permeation through the KcsA channel: a density functional study
    • Guidoni L., and Carloni P. Potassium permeation through the KcsA channel: a density functional study. Biochim. Biophys. Acta 1563 (2002) 1-6
    • (2002) Biochim. Biophys. Acta , vol.1563 , pp. 1-6
    • Guidoni, L.1    Carloni, P.2
  • 23
    • 3142652094 scopus 로고    scopus 로고
    • Theoretical and computational models of biological ion channels
    • Roux B., Allen T.W., Bernèche S., and Im W. Theoretical and computational models of biological ion channels. Q. Rev. Biophys. 37 (2004) 15-103
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 15-103
    • Roux, B.1    Allen, T.W.2    Bernèche, S.3    Im, W.4
  • 24
    • 0026471029 scopus 로고
    • Molecular determinants of channel function
    • Andersen O.S., and Koeppe R.E. Molecular determinants of channel function. Physiol. Rev. 72 (1992) S89-S158
    • (1992) Physiol. Rev. , vol.72
    • Andersen, O.S.1    Koeppe, R.E.2
  • 25
    • 0023709415 scopus 로고
    • Potassium blocks barium permeation through a calcium-activated potassium channel
    • Neyton J., and Miller C. Potassium blocks barium permeation through a calcium-activated potassium channel. J. Gen. Physiol. 92 (1988) 549-567
    • (1988) J. Gen. Physiol. , vol.92 , pp. 549-567
    • Neyton, J.1    Miller, C.2
  • 29
    • 31544436643 scopus 로고    scopus 로고
    • Incidence of partial charges on ion selectivity in potassium channels
    • Huetz P., Boiteux C., Compoint M., Ramseyer C., and Girardet C. Incidence of partial charges on ion selectivity in potassium channels. J. Chem. Phys. 124 (2006) 044703
    • (2006) J. Chem. Phys. , vol.124 , pp. 044703
    • Huetz, P.1    Boiteux, C.2    Compoint, M.3    Ramseyer, C.4    Girardet, C.5
  • 30
    • 0036714139 scopus 로고    scopus 로고
    • Na(+) block and permeation in a K(+) channel of known structure
    • Nimigean C., and Miller C. Na(+) block and permeation in a K(+) channel of known structure. J. Gen. Physiol. 120 (2002) 323-335
    • (2002) J. Gen. Physiol. , vol.120 , pp. 323-335
    • Nimigean, C.1    Miller, C.2
  • 31
    • 32044461366 scopus 로고
    • Studies of mechanism of ionic exchange in colloidal aluminum silicates
    • Jenny H. Studies of mechanism of ionic exchange in colloidal aluminum silicates. J. Phys. Chem. 36 (1932) 2217
    • (1932) J. Phys. Chem. , vol.36 , pp. 2217
    • Jenny, H.1
  • 32
    • 0000436463 scopus 로고
    • Thermochemistry and thermodynamics of ion exchange in crystalline exchange medium
    • Barrer R. Thermochemistry and thermodynamics of ion exchange in crystalline exchange medium. Proc. R. Soc. Lond., A Math. Phys. Sci. 273 (1963) 180-187
    • (1963) Proc. R. Soc. Lond., A Math. Phys. Sci. , vol.273 , pp. 180-187
    • Barrer, R.1
  • 33
    • 27644591457 scopus 로고
    • Studies of ion-exchange resins: selectivity coefficients of various cation exchangers towards univalent ions
    • Gregor H.P. Studies of ion-exchange resins: selectivity coefficients of various cation exchangers towards univalent ions. J. Coll. Sci. 6 (1951) 323
    • (1951) J. Coll. Sci. , vol.6 , pp. 323
    • Gregor, H.P.1
  • 35
    • 10344257941 scopus 로고
    • An analysis of pore size in excitable membranes
    • Mullins L.J. An analysis of pore size in excitable membranes. J. Gen. Physiol. 43 (1960) 105-117
    • (1960) J. Gen. Physiol. , vol.43 , pp. 105-117
    • Mullins, L.J.1
  • 36
    • 0014439655 scopus 로고
    • Biological membranes-physical basis of ion and nonelectrolyte selectivity
    • Diamond J.M., and Wright E.M. Biological membranes-physical basis of ion and nonelectrolyte selectivity. Annu. Rev. Physiol. 31 (1969) 581-646
    • (1969) Annu. Rev. Physiol. , vol.31 , pp. 581-646
    • Diamond, J.M.1    Wright, E.M.2
  • 37
    • 0014177657 scopus 로고
    • Effect of valinomycin on ionic permeability of thin lipid membranes
    • Andreoli T.E., Tieffenb M., and Tosteson D.C. Effect of valinomycin on ionic permeability of thin lipid membranes. J. Gen. Physiol. 50 (1967) 2527
    • (1967) J. Gen. Physiol. , vol.50 , pp. 2527
    • Andreoli, T.E.1    Tieffenb, M.2    Tosteson, D.C.3
  • 38
    • 0014212802 scopus 로고
    • + discrimination in experimental biomolecular lipid membranes by macrocyclic antibiotics
    • + discrimination in experimental biomolecular lipid membranes by macrocyclic antibiotics. Biochem. Biophys. Res. Commun. 26 (1967) 398
    • (1967) Biochem. Biophys. Res. Commun. , vol.26 , pp. 398
    • Mueller, P.1    Rudin, D.O.2
  • 39
    • 0002414822 scopus 로고
    • A theory for effects of neutral carriers such as macrotetralide actin antibiotics on electric properties of bilayer membranes
    • Ciani S., Eisenman G., and Szabo G. A theory for effects of neutral carriers such as macrotetralide actin antibiotics on electric properties of bilayer membranes. J. Membr. Biol. 1 (1969) 1-12
    • (1969) J. Membr. Biol. , vol.1 , pp. 1-12
    • Ciani, S.1    Eisenman, G.2    Szabo, G.3
  • 40
    • 33750622657 scopus 로고
    • Experimentally observed effects if carriers on the electrical properties of bilayer membranes-equilibrium domain
    • Eisenman G. (Ed), Marcel Dekker Inc., New York
    • Szabo G., Eisenman G., Laprade R., Ciani S.M., and Krasne S. Experimentally observed effects if carriers on the electrical properties of bilayer membranes-equilibrium domain. In: Eisenman G. (Ed). Membranes: A Series of Advances (1973), Marcel Dekker Inc., New York 291-328
    • (1973) Membranes: A Series of Advances , pp. 291-328
    • Szabo, G.1    Eisenman, G.2    Laprade, R.3    Ciani, S.M.4    Krasne, S.5
  • 41
    • 33750616752 scopus 로고
    • Ionic selectivity of proteins: lessons from molecular dynamics simulations on valinomycin
    • Gaber B.P., and Easwaran K.R.K. (Eds), Adenine Press
    • Eisenman G., and Alvarez O. Ionic selectivity of proteins: lessons from molecular dynamics simulations on valinomycin. In: Gaber B.P., and Easwaran K.R.K. (Eds). Biomembrane Structure and Functions: The State of the Art (1992), Adenine Press 321-351
    • (1992) Biomembrane Structure and Functions: The State of the Art , pp. 321-351
    • Eisenman, G.1    Alvarez, O.2
  • 42
    • 0021070747 scopus 로고
    • Ion selectivity revisited: the role of kinetic and equilibrium processes in ion permeation through channels
    • Eisenman G., and Horn R. Ion selectivity revisited: the role of kinetic and equilibrium processes in ion permeation through channels. J. Membr. Biol. 76 (1983) 197-225
    • (1983) J. Membr. Biol. , vol.76 , pp. 197-225
    • Eisenman, G.1    Horn, R.2
  • 44
    • 0015424492 scopus 로고
    • Negative conductance caused by entry of sodium and cesium ions into the potassium channels of squid axons
    • Bezanilla F., and Armstrong C.M. Negative conductance caused by entry of sodium and cesium ions into the potassium channels of squid axons. J. Gen. Physiol. 60 (1972) 588-608
    • (1972) J. Gen. Physiol. , vol.60 , pp. 588-608
    • Bezanilla, F.1    Armstrong, C.M.2
  • 45
    • 10344245541 scopus 로고    scopus 로고
    • On the importance of atomic fluctuations, protein flexibility and solvent in ion permeation
    • Allen T.W., Andersen O.S., and Roux B. On the importance of atomic fluctuations, protein flexibility and solvent in ion permeation. J. Gen. Physiol. 124 (2004) 679-690
    • (2004) J. Gen. Physiol. , vol.124 , pp. 679-690
    • Allen, T.W.1    Andersen, O.S.2    Roux, B.3
  • 47
    • 0034690250 scopus 로고    scopus 로고
    • Ion permeation mechanism of the potassium channel
    • Åqvist J., and Luzhkov V. Ion permeation mechanism of the potassium channel. Nature 404 (2000) 881-884
    • (2000) Nature , vol.404 , pp. 881-884
    • Åqvist, J.1    Luzhkov, V.2
  • 48
    • 0032750783 scopus 로고    scopus 로고
    • Molecular dynamics study of the KcsA potassium channel
    • Allen T.W., Kuyucak S., and Chung S.H. Molecular dynamics study of the KcsA potassium channel. Biophys. J. 77 (1999) 2502-2516
    • (1999) Biophys. J. , vol.77 , pp. 2502-2516
    • Allen, T.W.1    Kuyucak, S.2    Chung, S.H.3
  • 49
    • 0042213113 scopus 로고    scopus 로고
    • + channel in a bilayer membrane
    • + channel in a bilayer membrane. Biophys. J. 78 (2000) 2900-2917
    • (2000) Biophys. J. , vol.78 , pp. 2900-2917
    • Bernèche, S.1    Roux, B.2
  • 50
    • 0035830616 scopus 로고    scopus 로고
    • Potassium and sodium ions in a potassium channel studied by molecular dynamics simulations
    • Biggin P.C., Smith G.R., Shrivastava I., Choe S., and Sansom M.S. Potassium and sodium ions in a potassium channel studied by molecular dynamics simulations. Biochim. Biophys. Acta 1510 (2001) 1-9
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 1-9
    • Biggin, P.C.1    Smith, G.R.2    Shrivastava, I.3    Choe, S.4    Sansom, M.S.5
  • 51
    • 1042275568 scopus 로고    scopus 로고
    • Molecular dynamics study of the KcsA channel at 2.0-A resolution: stability and concerted motions within the pore
    • Compoint M., Carloni P., Ramseyer C., and Girardet C. Molecular dynamics study of the KcsA channel at 2.0-A resolution: stability and concerted motions within the pore. Biochim. Biophys. Acta 1661 (2004) 26-39
    • (2004) Biochim. Biophys. Acta , vol.1661 , pp. 26-39
    • Compoint, M.1    Carloni, P.2    Ramseyer, C.3    Girardet, C.4
  • 52
    • 0038009204 scopus 로고    scopus 로고
    • Potassium channel, ions, and water: simulation studies based on the high resolution X-ray structure of KcsA
    • Domene C., and Sansom M.S. Potassium channel, ions, and water: simulation studies based on the high resolution X-ray structure of KcsA. Biophys. J. 85 (2003) 2787-2800
    • (2003) Biophys. J. , vol.85 , pp. 2787-2800
    • Domene, C.1    Sansom, M.S.2
  • 55
    • 0034730689 scopus 로고    scopus 로고
    • A computational study of ion binding and protonation states in the KcsA potassium channel
    • Luzhkov V.B., and Åqvist J. A computational study of ion binding and protonation states in the KcsA potassium channel. Biochim. Biophys. Acta 1481 (2000) 360-370
    • (2000) Biochim. Biophys. Acta , vol.1481 , pp. 360-370
    • Luzhkov, V.B.1    Åqvist, J.2
  • 56
    • 0035855251 scopus 로고    scopus 로고
    • + selectivity of the KcsA potassium channel from microscopic free energy perturbation calculations
    • + selectivity of the KcsA potassium channel from microscopic free energy perturbation calculations. Biochim. Biophys. Acta 1548 (2001) 194-202
    • (2001) Biochim. Biophys. Acta , vol.1548 , pp. 194-202
    • Luzhkov, V.B.1    Åqvist, J.2
  • 57
    • 0034036372 scopus 로고    scopus 로고
    • Simulations of ion permeation through a potassium channel: molecular dynamics of KcsA in a phospholipid bilayer
    • Shrivastava I., and Sansom M. Simulations of ion permeation through a potassium channel: molecular dynamics of KcsA in a phospholipid bilayer. Biophys. J. 78 (2000) 557-570
    • (2000) Biophys. J. , vol.78 , pp. 557-570
    • Shrivastava, I.1    Sansom, M.2
  • 61
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • Gouaux E., and MacKinnon R. Principles of selective ion transport in channels and pumps. Science 310 (2005) 1461-1465
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    MacKinnon, R.2
  • 62
    • 33845378831 scopus 로고
    • Coordination chemistry of alkali and alkaline-earth cations with macrocyclic ligands
    • Dietrich B. Coordination chemistry of alkali and alkaline-earth cations with macrocyclic ligands. J. Chem. Educ. 62 (1985) 954-964
    • (1985) J. Chem. Educ. , vol.62 , pp. 954-964
    • Dietrich, B.1
  • 64
    • 0020247988 scopus 로고
    • Solution thermodynamics studies: 6. Enthalpy-entropy compensation for the complexation reaction of some crown ethers with alkaline cations. Quantitative interpretation of the complexing properties of 18 Crown-6
    • Michaux G., and Reisse J. Solution thermodynamics studies: 6. Enthalpy-entropy compensation for the complexation reaction of some crown ethers with alkaline cations. Quantitative interpretation of the complexing properties of 18 Crown-6. J. Am. Chem. Soc. 104 (1982) 6895-6899
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6895-6899
    • Michaux, G.1    Reisse, J.2
  • 65
    • 0020846719 scopus 로고
    • Clarification of the hole-size cation-diameter relationship in crown ethers and a new method for determining calcium cation homogeneous binding constant
    • Gokel G.W., Goli D.M., Mlinganti C., and Echegoyen L. Clarification of the hole-size cation-diameter relationship in crown ethers and a new method for determining calcium cation homogeneous binding constant. J. Am. Chem. Soc. 105 (1983) 6786-6788
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6786-6788
    • Gokel, G.W.1    Goli, D.M.2    Mlinganti, C.3    Echegoyen, L.4
  • 67
    • 7044239742 scopus 로고
    • Free energy calculations: applications to chemical and biochemical phenomena
    • Kollman P.A. Free energy calculations: applications to chemical and biochemical phenomena. Chem. Rev. 93 (1993) 2395-2417
    • (1993) Chem. Rev. , vol.93 , pp. 2395-2417
    • Kollman, P.A.1
  • 68
    • 36849122972 scopus 로고
    • High temperature equation of state by a perturbation method
    • Zwanzig R.W. High temperature equation of state by a perturbation method. J. Chem. Phys. 22 (1954) 1420-1426
    • (1954) J. Chem. Phys. , vol.22 , pp. 1420-1426
    • Zwanzig, R.W.1
  • 69
    • 0344796204 scopus 로고
    • Ion-water interaction potential derived from free energy perturbation simulations
    • Åqvist J. Ion-water interaction potential derived from free energy perturbation simulations. J. Phys. Chem. 94 (1990) 8021-8024
    • (1990) J. Phys. Chem. , vol.94 , pp. 8021-8024
    • Åqvist, J.1
  • 70
    • 0001655657 scopus 로고
    • Finite representation of an infinite bulk system: solvent boundary potential for computer simulations
    • Beglov D., and Roux B. Finite representation of an infinite bulk system: solvent boundary potential for computer simulations. J. Chem. Phys. 100 (1994) 9050-9063
    • (1994) J. Chem. Phys. , vol.100 , pp. 9050-9063
    • Beglov, D.1    Roux, B.2
  • 72
    • 0013780285 scopus 로고
    • Induced active transport of ions in mitochondria
    • Pressman B.C. Induced active transport of ions in mitochondria. Proc. Natl. Acad. Sci. U. S. A. 53 (1965) 1076-1080
    • (1965) Proc. Natl. Acad. Sci. U. S. A. , vol.53 , pp. 1076-1080
    • Pressman, B.C.1
  • 73
    • 0015524818 scopus 로고
    • Valinomycin crystal structure determination by direct methods
    • Duax W.L., Hauptman H., Weeks C.M., and Norton D.A. Valinomycin crystal structure determination by direct methods. Science 176 (1972) 911-914
    • (1972) Science , vol.176 , pp. 911-914
    • Duax, W.L.1    Hauptman, H.2    Weeks, C.M.3    Norton, D.A.4
  • 74
    • 84988087853 scopus 로고
    • The molecular mechanics of valinomycin
    • Masut R.A., and Kushick J.N. The molecular mechanics of valinomycin. J. Comput. Chem. 6 (1985) 148-155
    • (1985) J. Comput. Chem. , vol.6 , pp. 148-155
    • Masut, R.A.1    Kushick, J.N.2
  • 75
    • 0343619924 scopus 로고
    • Ion-selective properties of a small ionophore in methanol studied by free energy perturbation simulations
    • Aqvist J., Alvarez O., and Eisenman G. Ion-selective properties of a small ionophore in methanol studied by free energy perturbation simulations. J. Phys. Chem. 96 (1992) 10019-10025
    • (1992) J. Phys. Chem. , vol.96 , pp. 10019-10025
    • Aqvist, J.1    Alvarez, O.2    Eisenman, G.3
  • 79
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell A.D.J., et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem., B 102 (1998) 3586-3616
    • (1998) J. Phys. Chem., B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.J.1
  • 80
    • 0036195868 scopus 로고    scopus 로고
    • On the potential functions used in molecular dynamics simulations of ion channels
    • Roux B., and Berneche S. On the potential functions used in molecular dynamics simulations of ion channels. Biophys. J. 82 (2002) 1681-1684
    • (2002) Biophys. J. , vol.82 , pp. 1681-1684
    • Roux, B.1    Berneche, S.2


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