메뉴 건너뛰기




Volumn 95, Issue 5, 1998, Pages 649-655

Crystal structure and functional analysis of the HERG potassium channel N terminus: A eukaryotic PAS domain

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; POTASSIUM CHANNEL; POTASSIUM ION;

EID: 0032567106     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0092-8674(00)81635-9     Document Type: Article
Times cited : (380)

References (33)
  • 1
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D., and Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219-220.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-220
    • Bacon, D.1    Anderson, W.F.2
  • 2
    • 0030925238 scopus 로고    scopus 로고
    • A signal transducer for aerotaxis in Escherichia coll
    • Bibikov, S.I., Biran, R., Rudd, K.E., and Parkinson, J.S. (1997). A signal transducer for aerotaxis in Escherichia coll. J. Bacteriol. 179, 4075-4079.
    • (1997) J. Bacteriol. , vol.179 , pp. 4075-4079
    • Bibikov, S.I.1    Biran, R.2    Rudd, K.E.3    Parkinson, J.S.4
  • 3
    • 0029110488 scopus 로고
    • 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site and chromophore
    • Borgstahl, G.E.O., Williams, D.R., and Getzoff, ED. (1995). 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site and chromophore. Biochemistry 34, 6278-6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.O.1    Williams, D.R.2    Getzoff, E.D.3
  • 4
    • 0037877123 scopus 로고    scopus 로고
    • The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT
    • Brunger, A.T. (1996). X-PLOR (version 3.851) Manual. (The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT).
    • (1996) X-PLOR (Version 3.851) Manual
    • Brunger, A.T.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4, Collaborative computational project 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 6
    • 0028011373 scopus 로고
    • Mass-spectrometry - A useful tool for the protein X-ray crystallographer and nmr spectroscopist
    • Chait, B.T. (1994). Mass-spectrometry - a useful tool for the protein X-ray crystallographer and NMR spectroscopist. Structure 2, 465-467.
    • (1994) Structure , vol.2 , pp. 465-467
    • Chait, B.T.1
  • 8
    • 0028914969 scopus 로고
    • A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome
    • Curran, M.E., Splawski, I., Timothy, K.W., Vincent, G.M., Green, E.D., and Keating, M.T. (1995). A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell 80, 795-803.
    • (1995) Cell , vol.80 , pp. 795-803
    • Curran, M.E.1    Splawski, I.2    Timothy, K.W.3    Vincent, G.M.4    Green, E.D.5    Keating, M.T.6
  • 10
    • 0031459411 scopus 로고    scopus 로고
    • Molecular evolution of two vertebrate aryl hydrocarbon (dioxin) receptors (AHR1 and AHR2) and the PAS family
    • Hahn, M.E., Karchner, S.I., Shapiro, M.A., and Perera, S.A. (1997). Molecular evolution of two vertebrate aryl hydrocarbon (dioxin) receptors (AHR1 and AHR2) and the PAS family. Proc. Natl. Acad. Sci. USA 94, 13743-13748.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13743-13748
    • Hahn, M.E.1    Karchner, S.I.2    Shapiro, M.A.3    Perera, S.A.4
  • 11
    • 0027991446 scopus 로고
    • The FSSP data base of structurally aligned protein fold families
    • Holm, L., and Sander, C. (1994). The FSSP data base of structurally aligned protein fold families. Nucleic Acids Res. 22, 3600-3609.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 12
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in the models
    • Jones, T.A., Zou, J.Y., Cowan, S., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in the models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 13
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 14
    • 0032580205 scopus 로고    scopus 로고
    • Crystal structure of the tetramerization domain of the shaker potassium channel
    • Kreusch, A., Pfaffinger, P.J., Stevens, C.F., and Choe, S. (1998). Crystal structure of the tetramerization domain of the Shaker potassium channel. Nature 392, 945-948.
    • (1998) Nature , vol.392 , pp. 945-948
    • Kreusch, A.1    Pfaffinger, P.J.2    Stevens, C.F.3    Choe, S.4
  • 15
    • 0030614462 scopus 로고    scopus 로고
    • The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression
    • Li, X., Xu, J., and Li, M. (1997). The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression. J. Biol. Chem. 272, 705-708.
    • (1997) J. Biol. Chem. , vol.272 , pp. 705-708
    • Li, X.1    Xu, J.2    Li, M.3
  • 16
    • 0030815133 scopus 로고    scopus 로고
    • RASTER3D: Photorealistic molecular graphics
    • Merritt, E.A., and Bacon, D.J. (1997). RASTER3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 17
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, and S. Bailey, eds. (Daresbury Laboratory, Daresbury, UK: Science and Engineering Research Council)
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing, L. Sawyer, N. Isaacs, and S. Bailey, eds. (Daresbury Laboratory, Daresbury, UK: Science and Engineering Research Council), pp. 56-62.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 18
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain super-family
    • Pellequer, J.-L., Wager-Smith, K.A., Kay, S.A., and Getzoff, E.D. (1998). Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain super-family. Proc. Natl. Acad. Sci. USA 95, 5884-5890.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5884-5890
    • Pellequer, J.-L.1    Wager-Smith, K.A.2    Kay, S.A.3    Getzoff, E.D.4
  • 19
    • 0031262875 scopus 로고    scopus 로고
    • PAS: A multifunctional domain family comes to light
    • Ponting, C.P., and Aravind, L. (1997). PAS: a multifunctional domain family comes to light. Curr. Biol. 7, R674-R677.
    • (1997) Curr. Biol. , vol.7
    • Ponting, C.P.1    Aravind, L.2
  • 20
    • 0030883388 scopus 로고    scopus 로고
    • The AER protein and the serine chemoreceptor TSR independently sense intracellular energy levels and transduce oxygen, redox and energy signals for Escherichia coll proc
    • Rebbapragada, A., Johnson, M.S., Harding, G.P., Zuccarelli, A.J., Fletcher, H.M., Zhulin, I., and Taylor, B.L. (1997). The AER protein and the serine chemoreceptor TSR independently sense intracellular energy levels and transduce oxygen, redox and energy signals for Escherichia coll Proc. Natl. Acad. Sci. USA 94, 10541-10546.
    • (1997) Natl. Acad. Sci. USA , vol.94 , pp. 10541-10546
    • Rebbapragada, A.1    Johnson, M.S.2    Harding, G.P.3    Zuccarelli, A.J.4    Fletcher, H.M.5    Zhulin, I.6    Taylor, B.L.7
  • 21
    • 0032125849 scopus 로고    scopus 로고
    • A clockwork explosion!
    • Reppert, S.M. (1998). A clockwork explosion! Cell 21, 1-4.
    • (1998) Cell , vol.21 , pp. 1-4
    • Reppert, S.M.1
  • 23
    • 0032580225 scopus 로고    scopus 로고
    • Molecular clocks: Mastering time by gene regulation
    • Sassone-Corsi, P. (1998). Molecular clocks: mastering time by gene regulation. Nature 392, 871-874.
    • (1998) Nature , vol.392 , pp. 871-874
    • Sassone-Corsi, P.1
  • 24
    • 0030054878 scopus 로고    scopus 로고
    • Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel
    • Schönherr, R., and Heinemann, S.H. (1996). Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel. J. Physiol. 493, 635-642.
    • (1996) J. Physiol. , vol.493 , pp. 635-642
    • Schönherr, R.1    Heinemann, S.H.2
  • 25
    • 0027971204 scopus 로고
    • Voltage gating of ion channels
    • Sigworth, F.J. (1994). Voltage gating of ion channels. Q. Rev. Biophys. 27, 1-40.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 1-40
    • Sigworth, F.J.1
  • 26
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90: Direct methods for larger structures
    • Sheldrick, G.M. (1990). Phase annealing in SHELX-90: direct methods for larger structures. Acta Crystallogr. 46, 467-473.
    • (1990) Acta Crystallogr. , vol.46 , pp. 467-473
    • Sheldrick, G.M.1
  • 27
    • 0030025308 scopus 로고    scopus 로고
    • The inward rectification mechanism of the HERG cardiac potassium channel
    • Smith, P.L., Baukrowitz, T., and Yellen, G. (1996). The inward rectification mechanism of the HERG cardiac potassium channel. Nature 379, 833-836.
    • (1996) Nature , vol.379 , pp. 833-836
    • Smith, P.L.1    Baukrowitz, T.2    Yellen, G.3
  • 29
    • 0030859332 scopus 로고    scopus 로고
    • Amino terminal-dependent gating of the potassium channel rat eag is compensated by a mutation in the S4 segment
    • Terlau, H., Heinemann, S.H., Stühmer, W., Pongs, O., and Ludwig, J. (1997). Amino terminal-dependent gating of the potassium channel rat eag is compensated by a mutation in the S4 segment. J. Physiol. 502, 537-543.
    • (1997) J. Physiol. , vol.502 , pp. 537-543
    • Terlau, H.1    Heinemann, S.H.2    Stühmer, W.3    Pongs, O.4    Ludwig, J.5
  • 30
    • 0029007356 scopus 로고
    • HERG, a human inward rectifier in the voltage-gated potassium channel family
    • Trudeau, M.C., Warmke, J.W., Ganetzky, B., and Robertson, G.A. (1995). HERG, a human inward rectifier in the voltage-gated potassium channel family. Science 269, 92-95.
    • (1995) Science , vol.269 , pp. 92-95
    • Trudeau, M.C.1    Warmke, J.W.2    Ganetzky, B.3    Robertson, G.A.4
  • 31
    • 0028292927 scopus 로고
    • A family of potassium channel genes related to eag in drosophila and mammals
    • Warmke, J.W., and Ganetzky, B. (1994). A family of potassium channel genes related to eag in Drosophila and mammals. Proc. Natl. Acad. Sci. USA 91, 3438-3442.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3438-3442
    • Warmke, J.W.1    Ganetzky, B.2
  • 32
    • 0025910233 scopus 로고
    • A distinct potassium channel polypeptide by the Drosophila eag locus
    • Warmke, J.W., Drysdale, R., and Ganetzky, B. (1991). A distinct potassium channel polypeptide by the Drosophila eag locus. Science 252, 1560-1562.
    • (1991) Science , vol.252 , pp. 1560-1562
    • Warmke, J.W.1    Drysdale, R.2    Ganetzky, B.3
  • 33
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in Archae, Bacteria and sensors for oxygen and redox
    • Zhulin, I.B., Taylor, B.L., and Dixon, R. (1997). PAS domain S-boxes in Archae, Bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22, 331-333.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.