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Volumn 392, Issue 6679, 1998, Pages 945-948

Crystal structure of the tetramerization domain of the Shaker potassium channel

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM CHANNEL;

EID: 0032580205     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/31978     Document Type: Article
Times cited : (274)

References (30)
  • 1
    • 0021123234 scopus 로고
    • Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence
    • Noda, M, et al. Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence. Nature 312, 121-127 (1984).
    • (1984) Nature , vol.312 , pp. 121-127
    • Noda, M.1
  • 2
    • 0023261936 scopus 로고
    • Primary structure of the receptor for calcium channel blockers from skeletal muscle
    • Tanabe, T. et al. Primary structure of the receptor for calcium channel blockers from skeletal muscle. Nature 328, 313-318 (1987).
    • (1987) Nature , vol.328 , pp. 313-318
    • Tanabe, T.1
  • 3
    • 0023225798 scopus 로고
    • Cloning of genomic and Complementary DNA from Shaker, a putative potassium channel gene form Drosophila
    • Papazian, D. M., Schwarz, T. L., Tempel, B. L., Jan, Y. N. & Jan, Y. L. Cloning of genomic and Complementary DNA from Shaker, a putative potassium channel gene form Drosophila. Science 237, 749-753 (1987).
    • (1987) Science , vol.237 , pp. 749-753
    • Papazian, D.M.1    Schwarz, T.L.2    Tempel, B.L.3    Jan, Y.N.4    Jan, Y.L.5
  • 4
    • 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, 232-235 (1991).
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 6
    • 0026344794 scopus 로고
    • Annus mirabilis of potassium channels
    • 1990
    • Miller, C. 1990: Annus mirabilis of potassium channels. Science 252, 1092-1095 (1991).
    • (1991) Science , vol.252 , pp. 1092-1095
    • Miller, C.1
  • 8
    • 0026794064 scopus 로고
    • Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel
    • Li, M., Jan, Y. N. & Jan, L. Y. Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel. Science 257, 1225-1230 (1992).
    • (1992) Science , vol.257 , pp. 1225-1230
    • Li, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 9
    • 0024285862 scopus 로고
    • Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila
    • Schwarz, T. L., Tempel, B. L., Papazian, D. M., Jan, Y. N. & Jan, L. Y. Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila. Nature 331, 137-142 (1988).
    • (1988) Nature , vol.331 , pp. 137-142
    • Schwarz, T.L.1    Tempel, B.L.2    Papazian, D.M.3    Jan, Y.N.4    Jan, L.Y.5
  • 10
    • 0025297328 scopus 로고
    • + current diversity is produced by an extended gene family conserved in Drosophila and mouse
    • + current diversity is produced by an extended gene family conserved in Drosophila and mouse. Science 248, 599-603 (1990).
    • (1990) Science , vol.248 , pp. 599-603
    • Wei, A.1
  • 11
    • 0024449639 scopus 로고
    • Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain
    • Stümer, W. et al. Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain. EMBO J. 8, 3235-3244 (1989).
    • (1989) EMBO J. , vol.8 , pp. 3235-3244
    • Stümer, W.1
  • 12
    • 0027440362 scopus 로고
    • Protein structure comparison by alignments of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignments of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 13
    • 0028961335 scopus 로고
    • "SCOP": A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, S. T. & Chothia, C. "SCOP": a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, S.T.3    Chothia, C.4
  • 14
    • 0017881332 scopus 로고
    • The alpha-helix dipole and the properties of proteins
    • Hol, W. G., van Duijnen, P, T. & Berendsen, H. J. The alpha-helix dipole and the properties of proteins. Nature 273, 443-446 (1978).
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.1    Van Duijnen, P.T.2    Berendsen, H.J.3
  • 15
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivauon
    • Hoshi, T., Zagotta, W. N. & Aldrich, R. W. Biophysical and molecular mechanisms of Shaker potassium channel inactivauon. Science 250, 533-538 (1990).
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 16
    • 0027364807 scopus 로고
    • Functional stoichiometry of Shaker potassium channel inactivation
    • MacKinnon, R., Aldrich, R. W. & Lee, A. W. Functional stoichiometry of Shaker potassium channel inactivation. Science 262, 757-759 (1993).
    • (1993) Science , vol.262 , pp. 757-759
    • MacKinnon, R.1    Aldrich, R.W.2    Lee, A.W.3
  • 18
    • 0026806605 scopus 로고
    • + channel by ShakerB inactivating "ball" peptide
    • + channel by ShakerB inactivating "ball" peptide. Neuron 9, 237-245 (1992).
    • (1992) Neuron , vol.9 , pp. 237-245
    • Toro, L.1    Stefani, E.2    Latorre, R.3
  • 19
    • 0031030766 scopus 로고    scopus 로고
    • NMR structure of inactivation gates from mammalian voltage-dependent potassium channels
    • Antz, C. et al. NMR structure of inactivation gates from mammalian voltage-dependent potassium channels. Nature 385, 272-274 (1997).
    • (1997) Nature , vol.385 , pp. 272-274
    • Antz, C.1
  • 21
    • 0030795112 scopus 로고    scopus 로고
    • Gated access to the pore of a voltage-dependent K̊ channel
    • Liu, T., Holmgren, M., Jurman, M, E. & Yellen, G. Gated access to the pore of a voltage-dependent K̊ channel Neuron 19, 175-184 (1997).
    • (1997) Neuron , vol.19 , pp. 175-184
    • Liu, T.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 22
    • 0030059224 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • Mannuzzu, L. M., Moronne, M. M. & Isacoff, E. Y. Direct physical measure of conformational rearrangement underlying potassium channel gating. Science 271, 213-216 (1996).
    • (1996) Science , vol.271 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 23
    • 0002452464 scopus 로고
    • eds Swayer, L., Isaac, N. & Bailey, S. SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. in Data Collection and Processing (eds Swayer, L., Isaac, N. & Bailey, S.) 56-62 (SERC Daresbury Laboratory, Warrington, UK, 1993).
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 24
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W. A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58 (1991).
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 25
    • 0011021892 scopus 로고
    • The CCP4 Suite: Programs for Crystallography
    • Collaborative Computational Project, Number 4. The CCP4 Suite: Programs for Crystallography. Acta Crystallogr. D 50, 670-673 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 670-673
  • 26
    • 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., Cowan, S. W. & Kjelgard, M. W. 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    Cowan, S.W.3    Kjelgard, M.W.4
  • 27
    • 0037877123 scopus 로고    scopus 로고
    • Dept of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT
    • Brunger, A. T. X-PLOR Version 3.8 (Dept of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 1996).
    • (1996) X-PLOR Version 3.8
    • Brunger, A.T.1
  • 28
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 29
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S. V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138 (1993).
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 30
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struc. Funct. Genet. 11, 281-296 (1991).
    • (1991) Proteins Struc. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.