메뉴 건너뛰기




Volumn 39, Issue 3, 2003, Pages 467-481

Atomic proximity between S4 segment and pore domain in shaker potassium channels

Author keywords

[No Author keywords available]

Indexed keywords

CADMIUM; CYSTEINE; METAL ION; VOLTAGE GATED POTASSIUM CHANNEL; ZINC ION;

EID: 0042697277     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(03)00468-9     Document Type: Article
Times cited : (157)

References (71)
  • 1
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts I.L., Nadassy K., Wodak S.J. Analysis of zinc binding sites in protein crystal structures. Protein Sci. 7:1998;1700-1716.
    • (1998) Protein Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 3
    • 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
  • 4
    • 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
  • 5
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla F. The voltage sensor in voltage-dependent ion channels. Physiol. Rev. 80:2000;555-592.
    • (2000) Physiol. Rev. , vol.80 , pp. 555-592
    • Bezanilla, F.1
  • 6
    • 0036795297 scopus 로고    scopus 로고
    • Voltage sensor movements
    • Bezanilla F. Voltage sensor movements. J. Gen. Physiol. 120:2002;465-473.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 465-473
    • Bezanilla, F.1
  • 7
    • 0028213205 scopus 로고
    • + channels: II. The components of gating currents and a model of channel activation
    • + channels. II. The components of gating currents and a model of channel activation Biophys. J. 66:1994;1011-1021.
    • (1994) Biophys. J. , vol.66 , pp. 1011-1021
    • Bezanilla, F.1    Perozo, E.2    Stefani, E.3
  • 9
    • 0026489631 scopus 로고
    • Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping
    • Careaga C.L., Falke J.J. Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping. J. Mol. Biol. 226:1992;1219-1235.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 11
    • 0033576580 scopus 로고    scopus 로고
    • Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
    • Cha A., Snyder G.E., Selvin P.R., Bezanilla F. Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature. 402:1999;809-813.
    • (1999) Nature , vol.402 , pp. 809-813
    • Cha, A.1    Snyder, G.E.2    Selvin, P.R.3    Bezanilla, F.4
  • 16
    • 0036792837 scopus 로고    scopus 로고
    • Molecular models of voltage sensing
    • Gandhi C.S., Isacoff E.Y. Molecular models of voltage sensing. J. Gen. Physiol. 120:2002;455-463.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 455-463
    • Gandhi, C.S.1    Isacoff, E.Y.2
  • 17
    • 0031977220 scopus 로고    scopus 로고
    • Luminescence resonance energy transfer measurements in myosin
    • Getz E.B., Cooke R., Selvin P.R. Luminescence resonance energy transfer measurements in myosin. Biophys. J. 74:1998;2451-2458.
    • (1998) Biophys. J. , vol.74 , pp. 2451-2458
    • Getz, E.B.1    Cooke, R.2    Selvin, P.R.3
  • 18
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding M.M. Geometry of metal-ligand interactions in proteins. Acta Crystallogr. D. 57:2001;401-411.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 19
    • 0026560616 scopus 로고
    • The aromatic binding site for tetraethylammonium ion on potassium channels
    • Heginbotham L., MacKinnon R. 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
  • 21
    • 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. 21:1998;617-621.
    • (1998) Neuron , vol.21 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 23
    • 0036794098 scopus 로고    scopus 로고
    • Coupled movements in voltage-gated ion channels
    • Horn R. Coupled movements in voltage-gated ion channels. J. Gen. Physiol. 120:2002;449-453.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 449-453
    • Horn, R.1
  • 24
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi T., Zagotta W.N., Aldrich R.W. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 250:1990;533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 25
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • a
    • Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:2002;515-522. a.
    • (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
  • 29
    • 0029041299 scopus 로고
    • Engineering a metal binding site within a polytopic membrane protein, the lactose permease of Escherichia coli
    • Jung K., Voss J., He M., Hubbell W.L., Kaback H.R. Engineering a metal binding site within a polytopic membrane protein, the lactose permease of Escherichia coli. Biochemistry. 34:1995;6272-6277.
    • (1995) Biochemistry , vol.34 , pp. 6272-6277
    • Jung, K.1    Voss, J.2    He, M.3    Hubbell, W.L.4    Kaback, H.R.5
  • 30
    • 0028590042 scopus 로고
    • Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites
    • Keifer L.L., Fierke C.A. Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites. Biochemistry. 33:1994;15233-15240.
    • (1994) Biochemistry , vol.33 , pp. 15233-15240
    • Keifer, L.L.1    Fierke, C.A.2
  • 31
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt O., Grunert H.P., Hahn U. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene. 96:1990;125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.P.2    Hahn, U.3
  • 33
    • 0032894433 scopus 로고    scopus 로고
    • Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation
    • Ledwell J.L., Aldrich R.W. Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation. J. Gen. Physiol. 113:1999;389-414.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 389-414
    • Ledwell, J.L.1    Aldrich, R.W.2
  • 37
    • 0033601168 scopus 로고    scopus 로고
    • Defining proximity relationships in the tertiary structure of the dopamine transporter
    • Loland C.J., Norregaard L., Gether U. Defining proximity relationships in the tertiary structure of the dopamine transporter. J. Biol. Chem. 274:1999;36928-36934.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36928-36934
    • Loland, C.J.1    Norregaard, L.2    Gether, U.3
  • 39
    • 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. 413:2001;809-813.
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 42
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon R. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature. 350:1991;232-235.
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 44
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon R., Cohen S.L., Kuo A., Lee A., Chait B.T. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 280:1998;106-109.
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 46
    • 0031020241 scopus 로고    scopus 로고
    • Potassium channel α and β subunits assemble in the endoplasmic reticulum
    • Nagaya N., Papazian D.M. Potassium channel α and β subunits assemble in the endoplasmic reticulum. J. Biol. Chem. 272:1997;3022-3027.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3022-3027
    • Nagaya, N.1    Papazian, D.M.2
  • 49
    • 0036355083 scopus 로고    scopus 로고
    • What can be deduced about the structure of Shaker from available data?
    • Roux B. What can be deduced about the structure of Shaker from available data? Novartis Found. Symp. 245:2002;84-101.
    • (2002) Novartis Found. Symp. , vol.245 , pp. 84-101
    • Roux, B.1
  • 51
    • 0028175781 scopus 로고
    • Glycosylation of Shaker potassium channel protein in insect cell culture and in Xenopus oocytes
    • Santacruz-Toloza L., Huang Y., John S.A., Papazian D.M. Glycosylation of Shaker potassium channel protein in insect cell culture and in Xenopus oocytes. Biochemistry. 33:1994;5607-5613.
    • (1994) Biochemistry , vol.33 , pp. 5607-5613
    • Santacruz-Toloza, L.1    Huang, Y.2    John, S.A.3    Papazian, D.M.4
  • 52
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar G., Sommer S.S. The "megaprimer" method of site-directed mutagenesis. Biotechniques. 8:1990;404-407.
    • (1990) Biotechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 54
    • 0032476018 scopus 로고    scopus 로고
    • Subunit folding and assembly steps are interspersed during Shaker potassium channel biogenesis
    • Schulteis C.T., Nagaya N., Papazian D.M. Subunit folding and assembly steps are interspersed during Shaker potassium channel biogenesis. J. Biol. Chem. 273:1998;26210-26217.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26210-26217
    • Schulteis, C.T.1    Nagaya, N.2    Papazian, D.M.3
  • 55
    • 0031952461 scopus 로고    scopus 로고
    • Activation of Shaker potassium channels. III. An activation gating model for wild-type and V2 mutant channels
    • Schoppa N.E., Sigworth F.J. Activation of Shaker potassium channels. III. An activation gating model for wild-type and V2 mutant channels. J. Gen. Physiol. 111:1998;313-342.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 313-342
    • Schoppa, N.E.1    Sigworth, F.J.2
  • 56
    • 0036085517 scopus 로고    scopus 로고
    • Principles and biophysical applications of lanthanide-based probes
    • Selvin P.R. Principles and biophysical applications of lanthanide-based probes. Annu. Rev. Biophys. Biomol. Struct. 31:2002;275-302.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 275-302
    • Selvin, P.R.1
  • 58
    • 0033762050 scopus 로고    scopus 로고
    • 2+ modulates voltage-dependent activation in ether-à-go-go potassium channels by binding between transmembrane segments S2 and S3
    • 2+ modulates voltage-dependent activation in ether-à-go-go potassium channels by binding between transmembrane segments S2 and S3. J. Gen. Physiol. 116:2000;663-678.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 663-678
    • Silverman, W.R.1    Tang, C.-Y.2    Mock, A.F.3    Huh, K.-B.4    Papazian, D.M.5
  • 60
    • 0035078574 scopus 로고    scopus 로고
    • Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution
    • Sokolova O., Kolmakova-Partensky L., Grigorieff N. Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution. Structure. 9:2001;215-220.
    • (2001) Structure , vol.9 , pp. 215-220
    • Sokolova, O.1    Kolmakova-Partensky, L.2    Grigorieff, N.3
  • 63
    • 0030893809 scopus 로고    scopus 로고
    • Electrostatic interactions between transmembrane segments mediate folding of Shaker potassium channel subunits
    • Tiwari-Woodruff S.K., Schulteis C.T., Mock A.F., Papazian D.M. Electrostatic interactions between transmembrane segments mediate folding of Shaker potassium channel subunits. Biophys. J. 72:1997;1489-1500.
    • (1997) Biophys. J. , vol.72 , pp. 1489-1500
    • Tiwari-Woodruff, S.K.1    Schulteis, C.T.2    Mock, A.F.3    Papazian, D.M.4
  • 66
    • 0030983156 scopus 로고    scopus 로고
    • Topology of the P segments in the sodium channel pore revealed by cysteine mutagenesis
    • Yamagishi T., Janecki M., Marban E., Tomaselli G.F. Topology of the P segments in the sodium channel pore revealed by cysteine mutagenesis. Biophys. J. 73:1997;195-204.
    • (1997) Biophys. J. , vol.73 , pp. 195-204
    • Yamagishi, T.1    Janecki, M.2    Marban, E.3    Tomaselli, G.F.4
  • 70
    • 0029845542 scopus 로고    scopus 로고
    • Measurement of the movement of the S4 segment during activation of a voltage-gated potassium channel
    • Yusaf S.P., Wray D., Sivaprasadarao A. Measurement of the movement of the S4 segment during activation of a voltage-gated potassium channel. Pflüg. Arch. 433:1996;91-97.
    • (1996) Pflüg. Arch. , vol.433 , pp. 91-97
    • Yusaf, S.P.1    Wray, D.2    Sivaprasadarao, A.3
  • 71
    • 0028140472 scopus 로고
    • Shaker potassium channel gating. III: Evaluation of kinetic models for activation
    • Zagotta W.N., Hoshi T., Aldrich R.W. Shaker potassium channel gating. III. Evaluation of kinetic models for activation J. Gen. Physiol. 103:1994;321-362.
    • (1994) J. Gen. Physiol. , vol.103 , pp. 321-362
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.