메뉴 건너뛰기




Volumn 5, Issue 6, 1998, Pages 459-469

Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER; POTASSIUM CHANNEL; POTASSIUM ION; TETRAMER;

EID: 2642701712     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0698-459     Document Type: Article
Times cited : (286)

References (48)
  • 2
    • 0026344794 scopus 로고
    • 1990: Annus mirabilis of potassium channels
    • Miller, C. 1990: annus mirabilis of potassium channels. Science 252, 1092-1096 (1991).
    • (1991) Science , vol.252 , pp. 1092-1096
    • Miller, C.1
  • 3
    • 0028093476 scopus 로고
    • Potassium channels and their evolving gates
    • Jan, L.Y. & Jan, Y.N. Potassium channels and their evolving gates. Nature 371, 119-122 (1994).
    • (1994) Nature , vol.371 , pp. 119-122
    • Jan, L.Y.1    Jan, Y.N.2
  • 4
    • 0001847927 scopus 로고    scopus 로고
    • Cloned potassium channels from eukaryotes and prokaryotes
    • Jan, L.Y. & Jan, Y.N. Cloned potassium channels from eukaryotes and prokaryotes. Annu. Rev. Neurosci. 20, 91-123 (1997).
    • (1997) Annu. Rev. Neurosci. , vol.20 , pp. 91-123
    • Jan, L.Y.1    Jan, Y.N.2
  • 5
    • 0028841033 scopus 로고
    • A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans
    • Schrempf, H. et al. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 14, 5170-5178 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5170-5178
    • Schrempf, H.1
  • 8
    • 0030745896 scopus 로고    scopus 로고
    • + channel (SKC1): Oligomeric stoichiometry and stability
    • + channel (SKC1): Oligomeric stoichiometry and stability. Biochemistry 36, 10343-10352 (1997).
    • (1997) Biochemistry , vol.36 , pp. 10343-10352
    • Cortes, D.M.1    Perozo, E.2
  • 9
    • 0032548788 scopus 로고    scopus 로고
    • + channel (SKC1): Secondary structure characterization from FTIR spertroscopy
    • + channel (SKC1): Secondary structure characterization from FTIR spertroscopy. FEBS Lett. 423, 205-212 (1998).
    • (1998) FEBS Lett. , vol.423 , pp. 205-212
    • Tatulian, S.A.1    Cortes, D.M.2    Perozo, E.3
  • 11
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280, 69-77 (1998).
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 14
    • 0023815085 scopus 로고
    • Structure of a bacterial sensory receptor. A site-directed sulfhydryl study
    • Falke, J.J. et al. Structure of a bacterial sensory receptor. A site-directed sulfhydryl study. J. Biol. Chem. 263, 14850-14858 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 14850-14858
    • Falke, J.J.1
  • 15
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein, M.D. & Shin, Y.K. Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. USA 92, 8239-8243 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 16
    • 0030950516 scopus 로고    scopus 로고
    • Molecular distances from dipolar coupled spin-labels - The global analysis of multifrequency continuous wave electron paramagnetic resonance data
    • Hustedt, E.J., Smirnov, A.I., Laub, C.F., Cobb, C.E. & Beth, A.H. Molecular distances from dipolar coupled spin-labels - the global analysis of multifrequency continuous wave electron paramagnetic resonance data. Biophys. J. 72, 1861-1877 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 1861-1877
    • Hustedt, E.J.1    Smirnov, A.I.2    Laub, C.F.3    Cobb, C.E.4    Beth, A.H.5
  • 17
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • Mchaourab, H.S., Oh, K.J., Fang, C.J. & Hubbell, W.L. Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry 36, 307-316 (1997).
    • (1997) Biochemistry , vol.36 , pp. 307-316
    • Mchaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 18
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach, C., Marti, T., Khorana, H.G. & Hubbell, W.L. Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science 248, 1088-1092 (1990).
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 19
    • 0027447891 scopus 로고
    • Colicin E1 binding to membranes: Time-resolved studies of spin-labeled mutants
    • Shin, Y.K., Levinthal, C., Levinthal, F. & Hubbell, W.L. Colicin E1 binding to membranes: time-resolved studies of spin-labeled mutants. Science 259, 960-963 (1993).
    • (1993) Science , vol.259 , pp. 960-963
    • Shin, Y.K.1    Levinthal, C.2    Levinthal, F.3    Hubbell, W.L.4
  • 20
    • 0027972897 scopus 로고
    • Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin
    • Steinhoff, H.J. et al. Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin. Science 266, 105-107 (1994).
    • (1994) Science , vol.266 , pp. 105-107
    • Steinhoff, H.J.1
  • 21
    • 0001350946 scopus 로고    scopus 로고
    • Organization of diphtheria toxin T domain in bilayers: A site-directed spin labeling study
    • Oh, K.J. et al. Organization of diphtheria toxin T domain in bilayers: a site-directed spin labeling study. Science 273, 810-812 (1996).
    • (1996) Science , vol.273 , pp. 810-812
    • Oh, K.J.1
  • 22
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D.L., Altenbach, C., Yang, K., Hubbell, W.L. & Khorana, H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770 (1996).
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 23
    • 0019874035 scopus 로고
    • The diffusion-concentration product of oxygen in lipid bilayers using the spin-label T1 method
    • Subczynski, W.K. & Hyde, J.S. The diffusion-concentration product of oxygen in lipid bilayers using the spin-label T1 method. Biochim. Biophys. Acta 643, 283-291 (1981).
    • (1981) Biochim. Biophys. Acta , vol.643 , pp. 283-291
    • Subczynski, W.K.1    Hyde, J.S.2
  • 24
    • 0024787356 scopus 로고
    • Conformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance
    • Altenbach, C., Froncisz, W., Hyde, J.S. & Hubbell, W.L. Conformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance. Biophys. J. 56, 1183-1191 (1989).
    • (1989) Biophys. J. , vol.56 , pp. 1183-1191
    • Altenbach, C.1    Froncisz, W.2    Hyde, J.S.3    Hubbell, W.L.4
  • 25
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H.S., Lietzow, M.A., Hideg, K. & Hubbell, W.L. Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35, 7692-7704 (1996).
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 26
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg, D., Weiss, R.M. & Terwilliger, T.C. The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. USA 81, 140-144 (1984).
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 27
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J.L. et al. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195, 659-685 (1987).
    • (1987) J. Mol. Biol. , vol.195 , pp. 659-685
    • Cornette, J.L.1
  • 28
    • 0028346566 scopus 로고
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: Application to spin-labeled mutants of bacteriorhodopsin
    • Altenbach, C., Greenhalgh, D.A., Khorana, H.G. & Hubbell, W.L. A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 91, 1667-1671 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 29
    • 0015255586 scopus 로고
    • Possibility of determining the distances between the functional groups of proteins by the method of paramagnetic labels
    • Kulikov, A.V., Likhtenshtein, G.I., Rozantsev, E.G. & Suskina, V.I. Possibility of determining the distances between the functional groups of proteins by the method of paramagnetic labels. Biofizika 17, 42-48 (1972).
    • (1972) Biofizika , vol.17 , pp. 42-48
    • Kulikov, A.V.1    Likhtenshtein, G.I.2    Rozantsev, E.G.3    Suskina, V.I.4
  • 30
    • 0030956162 scopus 로고    scopus 로고
    • + channels: Evidence for a trap door mechanism of activation gating
    • + channels: evidence for a trap door mechanism of activation gating. J. Gen. Phys. 109, 527-535 (1997).
    • (1997) J. Gen. Phys. , vol.109 , pp. 527-535
    • Holmgren, M.1    Smith, P.L.2    Yellen, G.3
  • 32
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins - The helical lattice superposition model
    • Walther, D., Eisenhaber, F. & Argos, P. Principles of helix-helix packing in proteins - the helical lattice superposition model. J. Mol. Biol. 255, 536-553 (1996).
    • (1996) J. Mol. Biol. , vol.255 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3
  • 33
    • 0030683493 scopus 로고    scopus 로고
    • Helix packing angle preferences
    • Bowie, J.U. Helix packing angle preferences. Nature Struct. Biol. 4, 915-917 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 915-917
    • Bowie, J.U.1
  • 34
    • 0031551579 scopus 로고    scopus 로고
    • Helix-helix packing in a membrane-like environment
    • Mingarro, I., Elofsson, A. & Vonheijne, G. Helix-helix packing in a membrane-like environment. J. Mol. Biol. 272, 633-641 (1997).
    • (1997) J. Mol. Biol. , vol.272 , pp. 633-641
    • Mingarro, I.1    Elofsson, A.2    Vonheijne, G.3
  • 35
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M.L. Solvent-accessible surfaces of proteins and nucleic acids. Science 221, 709-713 (1983).
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 36
    • 0028115778 scopus 로고
    • + channel comprises part of the pore
    • + channel comprises part of the pore. Nature 367, 179-182 (1994).
    • (1994) Nature , vol.367 , pp. 179-182
    • Lopez, G.A.1    Jan, Y.N.2    Jan, L.Y.3
  • 37
    • 0027417650 scopus 로고
    • The internal quaternary ammonium receptor site of Shaker potassium channels
    • Choi, K.L., Mossman, C., Aube, J. & Yellen, G. The internal quaternary ammonium receptor site of Shaker potassium channels. Neuron 10, 533-541 (1993).
    • (1993) Neuron , vol.10 , pp. 533-541
    • Choi, K.L.1    Mossman, C.2    Aube, J.3    Yellen, G.4
  • 40
    • 0013975093 scopus 로고
    • Time course of TEA+-induced anomalous rectification in squid giant axons
    • Armstrong, C.M. Time course of TEA+-induced anomalous rectification in squid giant axons. J. Gen. Phys. 50, 491-503 (1966).
    • (1966) J. Gen. Phys. , vol.50 , pp. 491-503
    • Armstrong, C.M.1
  • 41
    • 0020366556 scopus 로고
    • Block of squid axon K channels by internally and externally applied barium ions
    • Armstrong, C.M., Swenson, R.P., Jr. & Taylor, S.R. Block of squid axon K channels by internally and externally applied barium ions. J. Gen. Phys. 80, 663-682 (1982).
    • (1982) J. Gen. Phys. , vol.80 , pp. 663-682
    • Armstrong, C.M.1    Swenson Jr., R.P.2    Taylor, S.R.3
  • 43
    • 0024549641 scopus 로고
    • Divalent ion trapping inside potassium channels of human T lymphocytes
    • Grissmer, S. & Cahalan, M.D. Divalent ion trapping inside potassium channels of human T lymphocytes. J. Gen. Phys. 93, 609-630 (1989).
    • (1989) J. Gen. Phys. , vol.93 , pp. 609-630
    • Grissmer, S.1    Cahalan, M.D.2
  • 44
    • 0030057048 scopus 로고    scopus 로고
    • Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating
    • Sun, Z.P., Akabas, M.H., Goulding, E.H., Karlin, A. & Siegelbaum, S.A. Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating. Neuron 16, 141-149 (1996).
    • (1996) Neuron , vol.16 , pp. 141-149
    • Sun, Z.P.1    Akabas, M.H.2    Goulding, E.H.3    Karlin, A.4    Siegelbaum, S.A.5
  • 45
    • 0021100259 scopus 로고
    • A simple and sensitive procedure for measuring isotope fluxes through ion-specific channels in heterogenous populations of membrane vesicles
    • Garty, H., Rudy, B. & Karlish, S.J. A simple and sensitive procedure for measuring isotope fluxes through ion-specific channels in heterogenous populations of membrane vesicles. J. Biol. Chem. 258, 13094-13099 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 13094-13099
    • Garty, H.1    Rudy, B.2    Karlish, S.J.3
  • 46
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W.J. & Schellman, J.A. Protein stability curves. Biopolymers 26, 1859-1877 (1987).
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 47
    • 0027016905 scopus 로고
    • Spin labeled cysteines as sensors for protein-lipid interaction and conformation in rhodopsin
    • Farahbakhsh, Z.T., Altenbach, C. & Hubbell, W.L. Spin labeled cysteines as sensors for protein-lipid interaction and conformation in rhodopsin. Photochemistry & Photobiology 56, 1019-1033 (1992).
    • (1992) Photochemistry & Photobiology , vol.56 , pp. 1019-1033
    • Farahbakhsh, Z.T.1    Altenbach, C.2    Hubbell, W.L.3
  • 48
    • 0028177302 scopus 로고
    • The prediction and orientation of alpha-helices from sequence alignments: The combined use of environment-dependent substitution tables, Fourier transform methods and helix capping rules
    • Donnelly, D., Overington, J.P. & Blundell, T.L. The prediction and orientation of alpha-helices from sequence alignments: the combined use of environment-dependent substitution tables, Fourier transform methods and helix capping rules. Prot. Engng. 7, 645-653 (1994).
    • (1994) Prot. Engng. , vol.7 , pp. 645-653
    • Donnelly, D.1    Overington, J.P.2    Blundell, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.