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Volumn 87, Issue 3, 2004, Pages 1526-1536

In silico activation of KcsA K+ channel by lateral forces applied to the C-termini of inner helices

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; GLYCINE; POTASSIUM CHANNEL; VALINE;

EID: 4444261061     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.037770     Document Type: Article
Times cited : (27)

References (41)
  • 1
    • 0016316437 scopus 로고
    • Ionic pores, gates, and gating currents
    • Armstrong, C. M. 1974. Ionic pores, gates, and gating currents. Q. Rev. Biophys. 7:179-210.
    • (1974) Q. Rev. Biophys. , vol.7 , pp. 179-210
    • Armstrong, C.M.1
  • 2
    • 0036156678 scopus 로고    scopus 로고
    • The ionization state and the conformation of Glu-71 in the KcsA K(+) channel
    • Bemeche, S., and B. Roux. 2002. The ionization state and the conformation of Glu-71 in the KcsA K(+) channel. Biophys. J. 82:772-780.
    • (2002) Biophys. J. , vol.82 , pp. 772-780
    • Bemeche, S.1    Roux, B.2
  • 3
    • 0036787715 scopus 로고    scopus 로고
    • Open-state models of a potassium channel
    • Biggin, P. C., and M. S. Sansom. 2002. Open-state models of a potassium channel. Biophys. J. 83:1867-1876.
    • (2002) Biophys. J. , vol.83 , pp. 1867-1876
    • Biggin, P.C.1    Sansom, M.S.2
  • 4
    • 26744440015 scopus 로고
    • Structural and energetic effects of truncating long ranged interactions in ionic polar fluids
    • Brooks, C. L., B. M. Pettitt, and M. Karplus. 1985. Structural and energetic effects of truncating long ranged interactions in ionic polar fluids. J. Chem. Phys. 83:5897-5908.
    • (1985) J. Chem. Phys. , vol.83 , pp. 5897-5908
    • Brooks, C.L.1    Pettitt, B.M.2    Karplus, M.3
  • 5
    • 0033576612 scopus 로고    scopus 로고
    • Functional characterization of a potassium-selective prokaryotic glutamate receptor
    • Chen, G. Q., C. Cui, M. L. Mayer, and E. Gouaux. 1999. Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature. 402:817-821.
    • (1999) Nature , vol.402 , pp. 817-821
    • Chen, G.Q.1    Cui, C.2    Mayer, M.L.3    Gouaux, E.4
  • 8
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz, J. D. 1995. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2:709-712.
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 9
    • 0141754098 scopus 로고    scopus 로고
    • Gating of MscL studied by steered molecular dynamics
    • Gullingsrud, J., and K. Schulten. 2003. Gating of MscL studied by steered molecular dynamics. Biophys. J. 85:2087-2099.
    • (2003) Biophys. J. , vol.85 , pp. 2087-2099
    • Gullingsrud, J.1    Schulten, K.2
  • 12
    • 0032168179 scopus 로고    scopus 로고
    • + channel can be trapped in the open state by an intersubunit metal bridge
    • + channel can be trapped in the open state by an intersubunit metal bridge. Neuron. 21:617-621.
    • (1998) Neuron , vol.21 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 15
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B. T. Chait, and R. MacKinnon. 2002b. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 17
    • 0037088901 scopus 로고    scopus 로고
    • The NMDA receptor M3 segment is a conserved transduction element coupling ligand binding to channel opening
    • Jones, K. S., H. M. VanDongen, and A. M. VanDongen. 2002. The NMDA receptor M3 segment is a conserved transduction element coupling ligand binding to channel opening. J. Neurosci. 22:2044-2053.
    • (2002) J. Neurosci. , vol.22 , pp. 2044-2053
    • Jones, K.S.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 18
    • 0036181719 scopus 로고    scopus 로고
    • Channel blockers acting at N-methyl-D-aspartate receptors: Differential effects of mutations in the vestibule and ion channel pore
    • Kashiwagi, K., T. Masuko, C. D. Nguyen, T. Kuno, I. Tanaka, K. Igarashi, and K. Williams. 2002. Channel blockers acting at N-methyl-D-aspartate receptors: differential effects of mutations in the vestibule and ion channel pore. Mol. Pharmacol. 61:533-545.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 533-545
    • Kashiwagi, K.1    Masuko, T.2    Nguyen, C.D.3    Kuno, T.4    Tanaka, I.5    Igarashi, K.6    Williams, K.7
  • 19
    • 0037387189 scopus 로고    scopus 로고
    • Potassium channel gating observed with site-directed mass tagging
    • Kelly, B. L., and A. Gross. 2003. Potassium channel gating observed with site-directed mass tagging. Nat. Struct. Biol. 10:280-284.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 280-284
    • Kelly, B.L.1    Gross, A.2
  • 20
    • 0034114521 scopus 로고    scopus 로고
    • Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties
    • Kohda, K., Y. Wang, and M. Yuzaki. 2000. Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties. Nat. Neurosci. 3:315-322.
    • (2000) Nat. Neurosci. , vol.3 , pp. 315-322
    • Kohda, K.1    Wang, Y.2    Yuzaki, M.3
  • 22
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis, T., and M. Karplus. 1999. Effective energy function for proteins in solution. Proteins. 35:133-152.
    • (1999) Proteins , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 23
    • 0023430366 scopus 로고
    • Monte Carlo-minimization approach to the multiple-minima problem in protein folding
    • Li, Z., and H. A. Scheraga. 1987. Monte Carlo-minimization approach to the multiple-minima problem in protein folding. Proc. Natl. Acad. Sci. USA. 84:6611-6615.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6611-6615
    • Li, Z.1    Scheraga, H.A.2
  • 24
    • 0030795112 scopus 로고    scopus 로고
    • Gated access to the pore of a voltage-dependent K+ channel
    • Liu, Y., M. Holmgren, M. E. Jurman, and G. Yellen. 1997. Gated access to the pore of a voltage-dependent K+ channel. Neuron. 19:175-184.
    • (1997) Neuron , vol.19 , pp. 175-184
    • Liu, Y.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 26
    • 0034730689 scopus 로고    scopus 로고
    • A computational study of ion binding and protonation states in the KcsA potassium channel
    • Luzhkov, V. B., and J. Aqvist. 2000. A computational study of ion binding and protonation states in the KcsA potassium channel. Blochim. Biophys. Acta. 1481:360-370.
    • (2000) Blochim. Biophys. Acta , vol.1481 , pp. 360-370
    • Luzhkov, V.B.1    Aqvist, J.2
  • 27
    • 5944250450 scopus 로고
    • Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials of the naturally occurring amino acids
    • Momany, F. A., R. F. McGuire, A. W. Burgess, and H. A. Scheraga. 1975. Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials of the naturally occurring amino acids. J. Phys. Chem. 79:2361-2381.
    • (1975) J. Phys. Chem. , vol.79 , pp. 2361-2381
    • Momany, F.A.1    McGuire, R.F.2    Burgess, A.W.3    Scheraga, H.A.4
  • 30
    • 0034744617 scopus 로고    scopus 로고
    • Coupling Gbetagamma-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels
    • Sadja, R., K. Smadja, N. Alagem, and E. Reuveny. 2001. Coupling Gbetagamma-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels. Neuron. 29:669-680.
    • (2001) Neuron , vol.29 , pp. 669-680
    • Sadja, R.1    Smadja, K.2    Alagem, N.3    Reuveny, E.4
  • 31
    • 0034030664 scopus 로고    scopus 로고
    • Structure and dynamics of K channel pore-lining helices: A comparative simulation study
    • Shrivastava, I. H., C. E. Capener, L. R. Forrest, and M. S. Sansom. 2000. Structure and dynamics of K channel pore-lining helices: a comparative simulation study. Biophys. J. 78:79-92.
    • (2000) Biophys. J. , vol.78 , pp. 79-92
    • Shrivastava, I.H.1    Capener, C.E.2    Forrest, L.R.3    Sansom, M.S.4
  • 32
    • 0034036372 scopus 로고    scopus 로고
    • Simulations of ion permeation through a potassium channel: Molecular dynamics of KcsA in a phospholipid bilayer
    • Shrivastava, I. H., and M. S. Sansom. 2000. Simulations of ion permeation through a potassium channel: molecular dynamics of KcsA in a phospholipid bilayer. Biophys. J. 78:557-570.
    • (2000) Biophys. J. , vol.78 , pp. 557-570
    • Shrivastava, I.H.1    Sansom, M.S.2
  • 33
    • 0242498592 scopus 로고    scopus 로고
    • Constitutive activation of the Shaker Kv channel
    • Sukhareva, M., D. H. Hackos, and K. J. Swartz. 2003. Constitutive activation of the Shaker Kv channel. J. Gen. Physiol. 122:541-556.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 541-556
    • Sukhareva, M.1    Hackos, D.H.2    Swartz, K.J.3
  • 36
    • 0035049090 scopus 로고    scopus 로고
    • Yeast screen for constitutively active mutant G protein-activated potassium channels
    • Yi, B. A., Y. F. Lin, Y. N. Jan, and L. Y. Jan. 2001. Yeast screen for constitutively active mutant G protein-activated potassium channels. Neuron. 29:657-667.
    • (2001) Neuron , vol.29 , pp. 657-667
    • Yi, B.A.1    Lin, Y.F.2    Jan, Y.N.3    Jan, L.Y.4
  • 38
    • 0001934359 scopus 로고
    • Vector method for calculating derivatives of energy of atom-atom interactions of complex molecules according to generalized coordinates
    • Zhorov, B. S. 1981. Vector method for calculating derivatives of energy of atom-atom interactions of complex molecules according to generalized coordinates. J. Struct. Chem. 22:4-8.
    • (1981) J. Struct. Chem. , vol.22 , pp. 4-8
    • Zhorov, B.S.1
  • 40
    • 0034003769 scopus 로고    scopus 로고
    • Monte Carlo-minimized energy profile of estradiol in the ligand-binding tunnel of 17 beta-hydroxysteroid dehydrogenase: Atomic mechanisms of steroid recognition
    • Zhorov, B. S., and S.-X. Lin. 2000. Monte Carlo-minimized energy profile of estradiol in the ligand-binding tunnel of 17 beta-hydroxysteroid dehydrogenase: atomic mechanisms of steroid recognition. Proteins. 38:414-427.
    • (2000) Proteins , vol.38 , pp. 414-427
    • Zhorov, B.S.1    Lin, S.-X.2
  • 41
    • 1042266533 scopus 로고    scopus 로고
    • Potassium, sodium, calcium, and glutamate-gated channels: Pore architecture and ligand action
    • Zhorov, B. S., and D. B. Tikhonov. 2004. Potassium, sodium, calcium, and glutamate-gated channels: pore architecture and ligand action. J. Neurochem. 88:782-799.
    • (2004) J. Neurochem. , vol.88 , pp. 782-799
    • Zhorov, B.S.1    Tikhonov, D.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.