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Volumn 20, Issue 8, 2012, Pages 1332-1342

Mechanism of Cd 2+ coordination during slow inactivation in potassium channels

Author keywords

[No Author keywords available]

Indexed keywords

CADMIUM; COORDINATION COMPOUND; CYSTEINE; DIMER; POTASSIUM CHANNEL; TETRAMER; BACTERIAL PROTEIN; LIPOSOME; PROKARYOTIC POTASSIUM CHANNEL;

EID: 84864844984     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.03.027     Document Type: Article
Times cited : (25)

References (60)
  • 2
    • 58149250085 scopus 로고    scopus 로고
    • High-resolution structure of the open NaK channel
    • A. Alam, and Y. Jiang High-resolution structure of the open NaK channel Nat. Struct. Mol. Biol. 16 2009 30 34
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 30-34
    • Alam, A.1    Jiang, Y.2
  • 3
    • 15244352867 scopus 로고    scopus 로고
    • The external TEA binding site and C-type inactivation in voltage-gated potassium channels
    • DOI 10.1529/biophysj.104.046664
    • P. Andalib, J.F. Consiglio, J.G. Trapani, and S.J. Korn The external TEA binding site and C-type inactivation in voltage-gated potassium channels Biophys. J. 87 2004 3148 3161 (Pubitemid 40468572)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 3148-3161
    • Andalib, P.1    Consiglio, J.F.2    Trapani, J.G.3    Korn, S.J.4
  • 4
    • 0028793256 scopus 로고
    • +]: A tale of two inactivation mechanisms
    • +]: a tale of two inactivation mechanisms Neuron 15 1995 951 960
    • (1995) Neuron , vol.15 , pp. 951-960
    • Baukrowitz, T.1    Yellen, G.2
  • 5
    • 34248995257 scopus 로고    scopus 로고
    • The action potential in mammalian central neurons
    • DOI 10.1038/nrn2148, PII NRN2148
    • B.P. Bean The action potential in mammalian central neurons Nat. Rev. Neurosci. 8 2007 451 465 (Pubitemid 46789230)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.6 , pp. 451-465
    • Bean, B.P.1
  • 6
    • 0042213113 scopus 로고    scopus 로고
    • + channel in a bilayer membrane
    • +) channel in a bilayer membrane Biophys. J. 78 2000 2900 2917 (Pubitemid 30396923)
    • (2000) Biophysical Journal , vol.78 , Issue.6 , pp. 2900-2917
    • Berneche, S.1    Roux, B.2
  • 7
    • 17044400911 scopus 로고    scopus 로고
    • A gate in the selectivity filter of potassium channels
    • S. Bernèche, and B. Roux A gate in the selectivity filter of potassium channels Structure 13 2005 591 600
    • (2005) Structure , vol.13 , pp. 591-600
    • Bernèche, S.1    Roux, B.2
  • 8
    • 33750530193 scopus 로고    scopus 로고
    • Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction
    • DOI 10.1085/jgp.200609638
    • R. Blunck, J.F. Cordero-Morales, L.G. Cuello, E. Perozo, and F. Bezanilla Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction J. Gen. Physiol. 128 2006 569 581 (Pubitemid 44664634)
    • (2006) Journal of General Physiology , vol.128 , Issue.5 , pp. 569-581
    • Blunck, R.1    Cordero-Morales, J.F.2    Cuello, L.G.3    Perozo, E.4    Bezanilla, F.5
  • 11
    • 0030840167 scopus 로고    scopus 로고
    • + channel with fluorescence
    • + channel with fluorescence Neuron 19 1997 1127 1140 (Pubitemid 27512372)
    • (1997) Neuron , vol.19 , Issue.5 , pp. 1127-1140
    • Cha, A.1    Bezanilla, F.2
  • 18
    • 79959655732 scopus 로고    scopus 로고
    • A multipoint hydrogen-bond network underlying KcsA C-type inactivation
    • J.F. Cordero-Morales, V. Jogini, S. Chakrapani, and E. Perozo A multipoint hydrogen-bond network underlying KcsA C-type inactivation Biophys. J. 100 2011 2387 2393
    • (2011) Biophys. J. , vol.100 , pp. 2387-2393
    • Cordero-Morales, J.F.1    Jogini, V.2    Chakrapani, S.3    Perozo, E.4
  • 19
    • 0030745896 scopus 로고    scopus 로고
    • + channel (SKC1): Oligomeric stoichiometry and stability
    • DOI 10.1021/bi971018y
    • + channel (SKC1): oligomeric stoichiometry and stability Biochemistry 36 1997 10343 10352 (Pubitemid 27357747)
    • (1997) Biochemistry , vol.36 , Issue.33 , pp. 10343-10352
    • Cortes, D.M.1    Perozo, E.2
  • 20
    • 77954485089 scopus 로고    scopus 로고
    • Structural mechanism of C-type inactivation in K(+) channels
    • L.G. Cuello, V. Jogini, D.M. Cortes, and E. Perozo Structural mechanism of C-type inactivation in K(+) channels Nature 466 2010 203 208
    • (2010) Nature , vol.466 , pp. 203-208
    • Cuello, L.G.1    Jogini, V.2    Cortes, D.M.3    Perozo, E.4
  • 22
    • 0026519665 scopus 로고
    • + channel correlate with occupancy of the pore
    • + channel correlate with occupancy of the pore Biophys. J. 61 1992 639 648
    • (1992) Biophys. J. , vol.61 , pp. 639-648
    • Demo, S.D.1    Yellen, G.2
  • 23
    • 3142545831 scopus 로고    scopus 로고
    • Metal ion effects on ion channel gating
    • DOI 10.1017/S0033583504003932
    • F. Elinder, and P. Arhem Metal ion effects on ion channel gating Q. Rev. Biophys. 36 2003 373 427 (Pubitemid 38902194)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.4 , pp. 373-427
    • Elinder, F.1    Arhem, P.2
  • 26
    • 0026560616 scopus 로고
    • The aromatic binding site for tetraethylammonium ion on potassium channels
    • L. Heginbotham, and R. MacKinnon The aromatic binding site for tetraethylammonium ion on potassium channels Neuron 8 1992 483 491
    • (1992) Neuron , vol.8 , pp. 483-491
    • Heginbotham, L.1    MacKinnon, R.2
  • 27
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • T. Hoshi, W.N. Zagotta, and R.W. Aldrich Biophysical and molecular mechanisms of Shaker potassium channel inactivation Science 250 1990 533 538 (Pubitemid 120031778)
    • (1990) Science , vol.250 , Issue.4980 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 28
    • 0026049511 scopus 로고
    • Two types of inactivation in Shaker K+ channels: Effects of alterations in the carboxy-terminal region
    • T. Hoshi, W.N. Zagotta, and R.W. Aldrich Two types of inactivation in Shaker K+ channels: effects of alterations in the carboxy-terminal region Neuron 7 1991 547 556
    • (1991) Neuron , vol.7 , pp. 547-556
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 29
    • 0027078418 scopus 로고
    • Cooperative interactions among subunits of a voltage-dependent potassium channel. Evidence from expression of concatenated cDNAs
    • R.S. Hurst, M.P. Kavanaugh, J. Yakel, J.P. Adelman, and R.A. North Cooperative interactions among subunits of a voltage-dependent potassium channel. Evidence from expression of concatenated cDNAs J. Biol. Chem. 267 1992 23742 23745 (Pubitemid 23088180)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.33 , pp. 23742-23745
    • Hurst, R.S.1    Kavanaugh, M.P.2    Yakel, J.3    Adelman, J.P.4    North, R.A.5
  • 30
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • DOI 10.1038/417523a
    • Y. Jiang, A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon The open pore conformation of potassium channels Nature 417 2002 523 526 (Pubitemid 34595913)
    • (2002) Nature , vol.417 , Issue.6888 , pp. 523-526
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 31
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 33745216690 scopus 로고    scopus 로고
    • A structural interpretation of voltage-gated potassium channel inactivation
    • H.T. Kurata, and D. Fedida A structural interpretation of voltage-gated potassium channel inactivation Prog. Biophys. Mol. Biol. 92 2006 185 208
    • (2006) Prog. Biophys. Mol. Biol. , vol.92 , pp. 185-208
    • Kurata, H.T.1    Fedida, D.2
  • 33
    • 0029990996 scopus 로고    scopus 로고
    • + channel during gating
    • DOI 10.1016/S0896-6273(00)80106-3
    • + channel during gating Neuron 16 1996 859 867 (Pubitemid 26124063)
    • (1996) Neuron , vol.16 , Issue.4 , pp. 859-867
    • Liu, Y.1    Jurman, M.E.2    Yellen, G.3
  • 35
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • DOI 10.1038/nsb1001-883
    • Y.-S. Liu, P. Sompornpisut, and E. Perozo Structure of the KcsA channel intracellular gate in the open state Nat. Struct. Biol. 8 2001 883 887 (Pubitemid 32923609)
    • (2001) Nature Structural Biology , vol.8 , Issue.10 , pp. 883-887
    • Liu, Y.-S.1    Sompornpisut, P.2    Perozo, E.3
  • 40
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • J. López-Barneo, T. Hoshi, S.H. Heinemann, and R.W. Aldrich Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels Receptors Channels 1 1993 61 71
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • López-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 41
    • 33746255471 scopus 로고    scopus 로고
    • String method in collective variables: Minimum free energy paths and isocommittor surfaces
    • L. Maragliano, A. Fischer, E. Vanden-Eijnden, and G. Ciccotti String method in collective variables: minimum free energy paths and isocommittor surfaces J. Chem. Phys. 125 2006 24106
    • (2006) J. Chem. Phys. , vol.125 , pp. 24106
    • Maragliano, L.1    Fischer, A.2    Vanden-Eijnden, E.3    Ciccotti, G.4
  • 42
    • 0028934109 scopus 로고
    • Three-dimensional solution structure of Callinectes sapidus metallothionein-1 determined by homonuclear and heteronuclear magnetic resonance spectroscopy
    • S.S. Narula, M. Brouwer, Y. Hua, and I.M. Armitage Three-dimensional solution structure of Callinectes sapidus metallothionein-1 determined by homonuclear and heteronuclear magnetic resonance spectroscopy Biochemistry 34 1995 620 631
    • (1995) Biochemistry , vol.34 , pp. 620-631
    • Narula, S.S.1    Brouwer, M.2    Hua, Y.3    Armitage, I.M.4
  • 45
    • 45949108535 scopus 로고    scopus 로고
    • Finding transition pathways using the string method with swarms of trajectories
    • A.C. Pan, D. Sezer, and B. Roux Finding transition pathways using the string method with swarms of trajectories J. Phys. Chem. B 112 2008 3432 3440
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3432-3440
    • Pan, A.C.1    Sezer, D.2    Roux, B.3
  • 47
    • 0033516494 scopus 로고    scopus 로고
    • +-channel activation gating
    • DOI 10.1126/science.285.5424.73
    • +-channel activation gating Science 285 1999 73 78 (Pubitemid 29307565)
    • (1999) Science , vol.285 , Issue.5424 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 50
    • 35348896761 scopus 로고    scopus 로고
    • Protein dynamics and monomer-monomer interactions in AntR activation by electron paramagnetic resonance and double electron-electron resonance
    • DOI 10.1021/bi700859p
    • K.I. Sen, T.M. Logan, and P.G. Fajer Protein dynamics and monomer-monomer interactions in AntR activation by electron paramagnetic resonance and double electron-electron resonance Biochemistry 46 2007 11639 11649 (Pubitemid 47585510)
    • (2007) Biochemistry , vol.46 , Issue.41 , pp. 11639-11649
    • Sen, K.I.1    Logan, T.M.2    Fajer, P.G.3
  • 52
    • 0030025308 scopus 로고    scopus 로고
    • The inward rectification mechanism of the HERG cardiac potassium channel
    • DOI 10.1038/379833a0
    • P.L. Smith, T. Baukrowitz, and G. Yellen The inward rectification mechanism of the HERG cardiac potassium channel Nature 379 1996 833 836 (Pubitemid 26067726)
    • (1996) Nature , vol.379 , Issue.6568 , pp. 833-836
    • Smith, P.L.1    Baukrowitz, T.2    Yellen, G.3
  • 53
    • 1242293628 scopus 로고    scopus 로고
    • The Outer Pore of the Glutamate Receptor Channel Has 2-Fold Rotational Symmetry
    • DOI 10.1016/S0896-6273(04)00008-X
    • A.I. Sobolevsky, M.V. Yelshansky, and L.P. Wollmuth The outer pore of the glutamate receptor channel has 2-fold rotational symmetry Neuron 41 2004 367 378 (Pubitemid 38221041)
    • (2004) Neuron , vol.41 , Issue.3 , pp. 367-378
    • Sobolevsky, A.I.1    Yelshansky, M.V.2    Wollmuth, L.P.3
  • 57
    • 0030906796 scopus 로고    scopus 로고
    • How does the W434F mutation block current in Shaker potassium channels?
    • DOI 10.1085/jgp.109.6.779
    • Y. Yang, Y. Yan, and F.J. Sigworth How does the W434F mutation block current in Shaker potassium channels? J. Gen. Physiol. 109 1997 779 789 (Pubitemid 27255942)
    • (1997) Journal of General Physiology , vol.109 , Issue.6 , pp. 779-789
    • Yang, Y.1    Yan, Y.2    Sigworth, F.J.3
  • 58
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • DOI 10.1017/S0033583598003448
    • G. Yellen The moving parts of voltage-gated ion channels Q. Rev. Biophys. 31 1998 239 295 (Pubitemid 29213771)
    • (1998) Quarterly Reviews of Biophysics , vol.31 , Issue.3 , pp. 239-295
    • Yellen, G.1
  • 59
    • 0028297301 scopus 로고
    • + channel allows inactivation to be modulated by metal binding
    • G. Yellen, D. Sodickson, T.-Y. Chen, and M.E. Jurman An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding Biophys. J. 66 1994 1068 1075 (Pubitemid 24106353)
    • (1994) Biophysical Journal , vol.66 , Issue.4 , pp. 1068-1075
    • Yellen, G.1    Sodickson, D.2    Chen, T.-Y.3    Jurman, M.E.4
  • 60
    • 0035499892 scopus 로고    scopus 로고
    • + channel-Fab complex at 2.0 A resolution
    • DOI 10.1038/35102009
    • Y. Zhou, J.H. Morais-Cabral, A. Kaufman, and R. MacKinnon Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution Nature 414 2001 43 48 (Pubitemid 33041616)
    • (2001) Nature , vol.414 , Issue.6859 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    Mackinnon, R.4


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