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Volumn 374, Issue 2, 2007, Pages 500-505

Direct Visualization of KirBac3.1 Potassium Channel Gating by Atomic Force Microscopy

Author keywords

atomic force microscopy; channel gating mechanism; conformational change; ligand binding; potassium channel

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; GUANINE NUCLEOTIDE BINDING PROTEIN; LIPID; MAGNESIUM ION; POTASSIUM CHANNEL; PROTEIN KIRBAC3.1; PROTON; UNCLASSIFIED DRUG;

EID: 35548982646     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.09.043     Document Type: Article
Times cited : (23)

References (31)
  • 1
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft F.M. From molecule to malady. Nature 440 (2006) 440-447
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 2
    • 3042695848 scopus 로고    scopus 로고
    • A family of putative Kir potassium channels in prokaryotes
    • Durell S.R., and Guy H.R. A family of putative Kir potassium channels in prokaryotes. BMC Evol. Biol. 1 (2001) 14
    • (2001) BMC Evol. Biol. , vol.1 , pp. 14
    • Durell, S.R.1    Guy, H.R.2
  • 3
    • 0344861820 scopus 로고    scopus 로고
    • Merging functional studies with structures of inward-rectifier K(+) channels
    • Bichet D., Haass F.A., and Jan L.Y. Merging functional studies with structures of inward-rectifier K(+) channels. Nature Rev. Neurosci. 4 (2003) 957-967
    • (2003) Nature Rev. Neurosci. , vol.4 , pp. 957-967
    • Bichet, D.1    Haass, F.A.2    Jan, L.Y.3
  • 4
    • 12444274301 scopus 로고    scopus 로고
    • Crystal structure of the potassium channel KirBac1.1 in the closed state
    • Kuo A., Gulbis J.M., Antcliff J.F., Rahman T., Lowe E.D., Zimmer J., et al. Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300 (2003) 1922-1926
    • (2003) Science , vol.300 , pp. 1922-1926
    • Kuo, A.1    Gulbis, J.M.2    Antcliff, J.F.3    Rahman, T.4    Lowe, E.D.5    Zimmer, J.6
  • 5
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 Å resolution
    • Nishida M., and MacKinnon R. Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 Å resolution. Cell 111 (2002) 957-965
    • (2002) Cell , vol.111 , pp. 957-965
    • Nishida, M.1    MacKinnon, R.2
  • 7
    • 34548386717 scopus 로고    scopus 로고
    • Crystal structure of a Kir3.1-prokaryotic Kir channel chimera
    • Nishida M., Cadene M., Chait B.T., and Mackinnon R. Crystal structure of a Kir3.1-prokaryotic Kir channel chimera. EMBO J. 26 (2007) 4005-4015
    • (2007) EMBO J. , vol.26 , pp. 4005-4015
    • Nishida, M.1    Cadene, M.2    Chait, B.T.3    Mackinnon, R.4
  • 9
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., and MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417 (2002) 515-522
    • (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
  • 10
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • Pegan S., Arrabit C., Zhou W., Kwiatkowski W., Collins A., Slesinger P.A., and Choe S. Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification. Nature Neurosci. 8 (2005) 279-287
    • (2005) Nature Neurosci. , vol.8 , pp. 279-287
    • Pegan, S.1    Arrabit, C.2    Zhou, W.3    Kwiatkowski, W.4    Collins, A.5    Slesinger, P.A.6    Choe, S.7
  • 11
    • 26444584556 scopus 로고    scopus 로고
    • Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography
    • Kuo A., Domene C., Johnson L.N., Doyle D.A., and Venien-Bryan C. Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography. Structure 13 (2005) 1463-1472
    • (2005) Structure , vol.13 , pp. 1463-1472
    • Kuo, A.1    Domene, C.2    Johnson, L.N.3    Doyle, D.A.4    Venien-Bryan, C.5
  • 13
    • 0042329979 scopus 로고    scopus 로고
    • Robert Feulgen Lecture. Microscopic assessment of membrane protein structure and function
    • Engel A. Robert Feulgen Lecture. Microscopic assessment of membrane protein structure and function. Histochem. Cell Biol. 120 (2003) 93-102
    • (2003) Histochem. Cell Biol. , vol.120 , pp. 93-102
    • Engel, A.1
  • 14
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy
    • Müller D.J., Fotiadis D., Scheuring S., Müller S.A., and Engel A. Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy. Biophys. J. 76 (1999) 1101-1111
    • (1999) Biophys. J. , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 15
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert F.A., Henn C., and Engel A. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science 268 (1995) 92-94
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 17
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • Scheuring S., and Sturgis J.N. Chromatic adaptation of photosynthetic membranes. Science 309 (2005) 484-487
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 18
    • 33846014316 scopus 로고    scopus 로고
    • The supramolecular architecture of junctional microdomains in native lens membranes
    • Buzhynskyy N., Hite R.K., Walz T., and Scheuring S. The supramolecular architecture of junctional microdomains in native lens membranes. EMBO Rep. 8 (2007) 51-55
    • (2007) EMBO Rep. , vol.8 , pp. 51-55
    • Buzhynskyy, N.1    Hite, R.K.2    Walz, T.3    Scheuring, S.4
  • 19
    • 0030596147 scopus 로고    scopus 로고
    • Surface topographies at sub-nanometer-resolution reveal asymmetry and sidedness of aquaporin-1
    • Walz T., Tittmann P., Fuchs K.H., Müller D.J., Smith B.L., Agre P., et al. Surface topographies at sub-nanometer-resolution reveal asymmetry and sidedness of aquaporin-1. J. Mol. Biol. 264 (1996) 907-918
    • (1996) J. Mol. Biol. , vol.264 , pp. 907-918
    • Walz, T.1    Tittmann, P.2    Fuchs, K.H.3    Müller, D.J.4    Smith, B.L.5    Agre, P.6
  • 25
    • 0036688712 scopus 로고    scopus 로고
    • New structural perspectives on K(+) channel gating
    • Perozo E. New structural perspectives on K(+) channel gating. Structure 10 (2002) 1027-1029
    • (2002) Structure , vol.10 , pp. 1027-1029
    • Perozo, E.1
  • 26
    • 17844380512 scopus 로고    scopus 로고
    • Conformational dynamics of the ligand-binding domain of inward rectifier K channels as revealed by molecular dynamics simulations: toward an understanding of Kir channel gating
    • Haider S., Grottesi A., Hall B.A., Ashcroft F.M., and Sansom M.S. Conformational dynamics of the ligand-binding domain of inward rectifier K channels as revealed by molecular dynamics simulations: toward an understanding of Kir channel gating. Biophys. J. 88 (2005) 3310-3320
    • (2005) Biophys. J. , vol.88 , pp. 3310-3320
    • Haider, S.1    Grottesi, A.2    Hall, B.A.3    Ashcroft, F.M.4    Sansom, M.S.5
  • 27
    • 33947709389 scopus 로고    scopus 로고
    • Molecular dynamics simulations of inwardly rectifying (Kir) potassium channels: a comparative study
    • Haider S., Khalid S., Tucker S.J., Ashcroft F.M., and Sansom M.S. Molecular dynamics simulations of inwardly rectifying (Kir) potassium channels: a comparative study. Biochemistry 46 (2007) 3643-3652
    • (2007) Biochemistry , vol.46 , pp. 3643-3652
    • Haider, S.1    Khalid, S.2    Tucker, S.J.3    Ashcroft, F.M.4    Sansom, M.S.5
  • 28
    • 0026095474 scopus 로고
    • Atomic force microscopy and dissection of gap junctions
    • Hoh J.H., Lal R., John S.A., Revel J.-P., and Arnsdorf M.F. Atomic force microscopy and dissection of gap junctions. Science 253 (1991) 1405-1408
    • (1991) Science , vol.253 , pp. 1405-1408
    • Hoh, J.H.1    Lal, R.2    John, S.A.3    Revel, J.-P.4    Arnsdorf, M.F.5
  • 29
    • 0037452675 scopus 로고    scopus 로고
    • Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core-complex in native membranes by AFM
    • Scheuring S., Seguin J., Marco S., Lévy D., Robert B., and Rigaud J.L. Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core-complex in native membranes by AFM. Proc. Natl. Acad. Sci. USA 100 (2003) 1690-1693
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1690-1693
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Lévy, D.4    Robert, B.5    Rigaud, J.L.6
  • 31
    • 34447638509 scopus 로고    scopus 로고
    • From high-resolution AFM topographs to atomic models of supramolecular assemblies
    • Scheuring S., Boudier T., and Sturgis J.N. From high-resolution AFM topographs to atomic models of supramolecular assemblies. J. Struct. Biol. 159 (2007) 268-276
    • (2007) J. Struct. Biol. , vol.159 , pp. 268-276
    • Scheuring, S.1    Boudier, T.2    Sturgis, J.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.