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Volumn 13, Issue 4, 2006, Pages 311-318

Molecular determinants of gating at the potassium-channel selectivity filter

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM CHANNEL; PROTON; VOLTAGE GATED POTASSIUM CHANNEL; BACTERIAL PROTEIN; PROKARYOTIC POTASSIUM CHANNEL; RECOMBINANT PROTEIN;

EID: 33745041507     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1069     Document Type: Article
Times cited : (379)

References (50)
  • 1
    • 4544342928 scopus 로고    scopus 로고
    • Potassium channels and the atomic basis of selective ion conduction
    • MacKinnon, R. Potassium channels and the atomic basis of selective ion conduction. Angew. Chem. Int. Edn Engl. 43, 4265-4277 (2004).
    • (2004) Angew. Chem. Int. Edn Engl. , vol.43 , pp. 4265-4277
    • MacKinnon, R.1
  • 2
    • 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, 35-42 (2002).
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 3
    • 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
  • 6
    • 33745055845 scopus 로고    scopus 로고
    • Voltage-dependent gating at the KcsA selectivity filter
    • advance online publication 12 March 2006 (doi:10.1038/nsmb1070)
    • Cordero, J.F., Cuello, L.G. & Perozo, E. Voltage-dependent gating at the KcsA selectivity filter. Nat. Struct. Mol. Biol., advance online publication 12 March 2006 (doi:10.1038/nsmb1070).
    • Nat. Struct. Mol. Biol.
    • Cordero, J.F.1    Cuello, L.G.2    Perozo, E.3
  • 7
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • Liu, Y.S., Sompornpisut, P. & Perozo, E. Structure of the KcsA channel intracellular gate in the open state. Nat. Struct. Biol. 8, 883-887 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 883-887
    • Liu, Y.S.1    Sompornpisut, P.2    Perozo, E.3
  • 11
    • 0036753545 scopus 로고    scopus 로고
    • + channel by pivoted bending of a transmembrane segment
    • + channel by pivoted bending of a transmembrane segment. Mol. Cell 10, 469-481 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 469-481
    • Jin, T.1
  • 14
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • Jiang, Y. et al. The open pore conformation of potassium channels. Nature 417, 523-526 (2002).
    • (2002) Nature , vol.417 , pp. 523-526
    • Jiang, Y.1
  • 15
    • 0038076054 scopus 로고    scopus 로고
    • + channel
    • + channel. Nature 423, 33-41 (2003).
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1
  • 16
    • 0032725268 scopus 로고    scopus 로고
    • Exploring the open pore of the potassium channel from Streptomyces lividans
    • Meuser, D., Splitt, H., Wagner, R. & Schrempf, H. Exploring the open pore of the potassium channel from Streptomyces lividans. FEBS Lett. 462, 447-452 (1999).
    • (1999) FEBS Lett. , vol.462 , pp. 447-452
    • Meuser, D.1    Splitt, H.2    Wagner, R.3    Schrempf, H.4
  • 17
    • 0026519665 scopus 로고
    • + channel correlate with occupancy of the pore
    • + channel correlate with occupancy of the pore. Biophys. J. 61, 639-648 (1992).
    • (1992) Biophys. J. , vol.61 , pp. 639-648
    • Demo, S.D.1    Yellen, G.2
  • 18
    • 0026328378 scopus 로고
    • Selectivity and gating of the type-L potassium channel in mouse lymphocytes
    • Shapiro, M.S. & Decoursey, T.E. Selectivity and gating of the type-L potassium channel in mouse lymphocytes. J. Gen. Physiol. 97, 1227-1250 (1991).
    • (1991) J. Gen. Physiol. , vol.97 , pp. 1227-1250
    • Shapiro, M.S.1    Decoursey, T.E.2
  • 19
    • 0024535492 scopus 로고
    • Rubidium ions and the gating of delayed rectifier potassium channels of frog skeletal-muscle
    • Spruce, A.E., Standen, N.B. & Stanfield, P.R. Rubidium ions and the gating of delayed rectifier potassium channels of frog skeletal-muscle. J. Physiol. (Lond.)411, 597-610 (1989).
    • (1989) J. Physiol. (Lond.) , vol.411 , pp. 597-610
    • Spruce, A.E.1    Standen, N.B.2    Stanfield, P.R.3
  • 20
    • 0019418315 scopus 로고
    • + channels close more slowly in the presence of external K+ and Rb+
    • + channels close more slowly in the presence of external K+ and Rb+. Nature 291, 427-429 (1981).
    • (1981) Nature , vol.291 , pp. 427-429
    • Swenson Jr., R.P.1    Armstrong, C.M.2
  • 21
    • 0035119276 scopus 로고    scopus 로고
    • + channel with backbone mutations in the selectivity filter
    • + channel with backbone mutations in the selectivity filter. Nat. Neurosci. 4, 239-246 (2001).
    • (2001) Nat. Neurosci. , vol.4 , pp. 239-246
    • Lu, T.1
  • 23
    • 0031022168 scopus 로고    scopus 로고
    • Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating
    • Chapman, M.L., VanDongen, H.M. & VanDongen, A.M. Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating. Biophys. J. 72, 708-719 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 708-719
    • Chapman, M.L.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 24
    • 0034774587 scopus 로고    scopus 로고
    • Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel
    • Proks, P., Capener, C.E., Jones, P. & Ashcroft, F.M. Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel. J. Gen. Physiol. 118, 341-353 (2001).
    • (2001) J. Gen. Physiol. , vol.118 , pp. 341-353
    • Proks, P.1    Capener, C.E.2    Jones, P.3    Ashcroft, F.M.4
  • 25
    • 0030818830 scopus 로고    scopus 로고
    • Selectivity changes during activation of mutant Shaker potassium channels
    • Zheng, J. & Sigworth, F.J. Selectivity changes during activation of mutant Shaker potassium channels. J. Gen. Physiol. 110, 101-117 (1997).
    • (1997) J. Gen. Physiol. , vol.110 , pp. 101-117
    • Zheng, J.1    Sigworth, F.J.2
  • 26
    • 0026049511 scopus 로고
    • + channels: Effects of alterations in the carboxy-terminal region
    • + channels: effects of alterations in the carboxy-terminal region. Neuron 7, 547-556 (1991).
    • (1991) Neuron , vol.7 , pp. 547-556
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 27
    • 0032907373 scopus 로고    scopus 로고
    • Contribution of the selectivity filter to inactivation in potassium channels
    • Kiss, L., LoTurco, J. & Korn, S.J. Contribution of the selectivity filter to inactivation in potassium channels. Biophys. J. 76, 253-263 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 253-263
    • Kiss, L.1    LoTurco, J.2    Korn, S.J.3
  • 29
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • Lopez-Barneo, J., Hoshi, T., Heinemann, S.H. & Aldrich, R.W. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels 1, 61-71 (1993).
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • Lopez-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 30
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Lu, Z., Klem, A.M. & Ramu, Y. Ion conduction pore is conserved among potassium channels. Nature 413, 809-813 (2001).
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 31
    • 29144472228 scopus 로고    scopus 로고
    • Activation-coupled inactivation in the bacterial potassium channel KcsA
    • Gao, L., Mi, X., Paajanen, V., Wang, K. & Fan, Z. Activation-coupled inactivation in the bacterial potassium channel KcsA. Proc. Natl. Acad. Sci. USA 102, 17630-17635 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17630-17635
    • Gao, L.1    Mi, X.2    Paajanen, V.3    Wang, K.4    Fan, Z.5
  • 33
    • 12444274301 scopus 로고    scopus 로고
    • Crystal structure of the potassium channel KirBac1.1 in the closed state
    • Kuo, A. et al. Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300, 1922-1926 (2003).
    • (2003) Science , vol.300 , pp. 1922-1926
    • Kuo, A.1
  • 34
    • 0031019498 scopus 로고    scopus 로고
    • Stabilization of ion selectivity filter by pore loop ion pairs in an inwardly rectifying potassium channel
    • Yang, J., Yu, M., Jan, Y.N. & Jan, L.Y. Stabilization of ion selectivity filter by pore loop ion pairs in an inwardly rectifying potassium channel. Proc. Natl. Acad. Sci. USA 94, 1568-1572 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1568-1572
    • Yang, J.1    Yu, M.2    Jan, Y.N.3    Jan, L.Y.4
  • 36
    • 0032559552 scopus 로고    scopus 로고
    • Molecular determinants of dofetilide block of HERG K+ channels
    • Ficker, E., Jarolimek, W., Kiehn, J., Baumann, A. & Brown, A.M. Molecular determinants of dofetilide block of HERG K+ channels. Circ. Res. 82, 386-395 (1998).
    • (1998) Circ. Res. , vol.82 , pp. 386-395
    • Ficker, E.1    Jarolimek, W.2    Kiehn, J.3    Baumann, A.4    Brown, A.M.5
  • 37
    • 0023053635 scopus 로고
    • Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation by molecular dynamics
    • Kuriyan, J., Petsko, G.A., Levy, R.M. & Karplus, M. Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation by molecular dynamics. J. Mol. Biol. 190, 227-254 (1986).
    • (1986) J. Mol. Biol. , vol.190 , pp. 227-254
    • Kuriyan, J.1    Petsko, G.A.2    Levy, R.M.3    Karplus, M.4
  • 38
    • 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
  • 39
    • 0035498860 scopus 로고    scopus 로고
    • Energetics of ion conduction through the K+ channel
    • Berneche, S. & Roux, B. Energetics of ion conduction through the K+ channel. Nature 414, 73-77 (2001).
    • (2001) Nature , vol.414 , pp. 73-77
    • Berneche, S.1    Roux, B.2
  • 40
    • 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, 965-975 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 965-975
    • Zhou, Y.1    MacKinnon, R.2
  • 42
    • 0024438904 scopus 로고
    • Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels
    • Delcour, A.H., Martinac, B., Adler, J. & Kung, C. Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels. Biophys. J. 56, 631-636 (1989).
    • (1989) Biophys. J. , vol.56 , pp. 631-636
    • Delcour, A.H.1    Martinac, B.2    Adler, J.3    Kung, C.4
  • 43
    • 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
  • 44
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D.M., Cuello, L.G. & Perozo, E. Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117, 165-180 (2001).
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowans, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowans, S.W.3    Kjeldgaard, M.4
  • 47
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T. et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 48
    • 0042213113 scopus 로고    scopus 로고
    • + channel in a bilayer membrane
    • + channel in a bilayer membrane. Biophys. J. 78, 2900-2917 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 2900-2917
    • Berneche, S.1    Roux, B.2
  • 49
    • 7044249333 scopus 로고    scopus 로고
    • Grand canonical Monte Carlo simulations of water in protein environments
    • Woo, H.J., Dinner, A.R. & Roux, B. Grand canonical Monte Carlo simulations of water in protein environments. J. Chem. Phys. 121, 6392-6400 (2004).
    • (2004) J. Chem. Phys. , vol.121 , pp. 6392-6400
    • Woo, H.J.1    Dinner, A.R.2    Roux, B.3
  • 50
    • 4444221565 scopus 로고    scopus 로고
    • Chimera - A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. Chimera - a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.