메뉴 건너뛰기




Volumn 60, Issue 8, 2003, Pages 1581-1590

The potassium channel KcsA and its interaction with the lipid bilayer

Author keywords

Fluorescence spectroscopy; KcsA; Lipid protein interactions; Potassium channel; Reconstitution; Tryptophan

Indexed keywords

CARBONYL DERIVATIVE; ION CHANNEL; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; POTASSIUM CHANNEL; POTASSIUM ION; PROTEIN KCSA; UNCLASSIFIED DRUG;

EID: 0041828861     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3172-y     Document Type: Review
Times cited : (41)

References (47)
  • 1
    • 0031922192 scopus 로고    scopus 로고
    • At last, the structure of an ion-selective channel
    • Clapham D. E. (1998) At last, the structure of an ion-selective channel. Nature Struct. Biol. 5: 342-344
    • (1998) Nature Struct. Biol. , vol.5 , pp. 342-344
    • Clapham, D.E.1
  • 4
    • 0035542975 scopus 로고    scopus 로고
    • Bacterial ion channels and their eukaryotic homologues
    • Koprowski P. and Kubalaski A. (2001) Bacterial ion channels and their eukaryotic homologues. Bioessays 23:1148-1158
    • (2001) Bioessays , vol.23 , pp. 1148-1158
    • Koprowski, P.1    Kubalaski, A.2
  • 5
    • 0028841033 scopus 로고
    • A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans
    • Schrempf H., Schmidt O., Kummerlen R., Hinnah,S., Muller D., Betzler M. et al. (1995) A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 14: 5170-5178
    • (1995) EMBO J. , vol.14 , pp. 5170-5178
    • Schrempf, H.1    Schmidt, O.2    Kummerlen, R.3    Hinnah, S.4    Muller, D.5    Betzler, M.6
  • 8
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Lu Z., Klem A. M. and Ramu Y. (2001) Ion conduction pore is conserved among potassium channels. Nature 413: 809-813
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 9
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of Type 1 single span membrane proteins
    • Landolt-Marticorena C., Williams K. A., Deber C. M. and Reithmeier R. A. F. (1993) Non-random distribution of amino acids in the transmembrane segments of Type 1 single span membrane proteins. J. Mol. Biol. 229: 602-608
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.F.4
  • 12
    • 0034036372 scopus 로고    scopus 로고
    • Simulations of ion permeation through a potassium channel: Molecular dynamics of KcsA in a phospholipid bilayer
    • Shrivastava I. H. and Sansom M. S. P. (2000) Simulations of ion permeation through a potassium channel: molecular dynamics of KcsA in a phospholipid bilayer. Biophys. J. 78: 557-570
    • (2000) Biophys. J. , vol.78 , pp. 557-570
    • Shrivastava, I.H.1    Sansom, M.S.P.2
  • 13
    • 0039179572 scopus 로고    scopus 로고
    • Ion channels, permeation, and electrostatics: Insights into the function of KcsA
    • Roux B., Berneche S. and Im W. (2000) Ion channels, permeation, and electrostatics: insights into the function of KcsA. Biochemistry 39: 13295-13306
    • (2000) Biochemistry , vol.39 , pp. 13295-13306
    • Roux, B.1    Berneche, S.2    Im, W.3
  • 15
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou M., Morais-Cabral J. H., Mann S. and Mackinnon R. (2001) Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature 411: 657-661
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    Mackinnon, R.4
  • 17
    • 0034730689 scopus 로고    scopus 로고
    • A computational study of ion binding and protonation states in the KcsA potassium channel
    • Luzhkov V. B. and Aqvist J. (2000) A computational study of ion binding and protonation states in the KcsA potassium channel. Biochim Biophys. Acta 1481: 360-370
    • (2000) Biochim Biophys. Acta , vol.1481 , pp. 360-370
    • Luzhkov, V.B.1    Aqvist, J.2
  • 20
    • 0034111512 scopus 로고    scopus 로고
    • Ion channels: Doing hard chemistry with hard ions
    • Miller C. (2000) Ion channels: doing hard chemistry with hard ions. Curr. Opin. Chem. Biol. 4: 148-151
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 148-151
    • Miller, C.1
  • 21
    • 0032725268 scopus 로고    scopus 로고
    • Exploring the open pore of the potassium channel from Streptomyces lividans
    • Meuser D., Splitt H., Wagner R. and Schrempf H. (1999) Exploring the open pore of the potassium channel from Streptomyces lividans. FEBS Lett. 462: 447-452
    • (1999) FEBS Lett. , vol.462 , pp. 447-452
    • Meuser, D.1    Splitt, H.2    Wagner, R.3    Schrempf, H.4
  • 23
    • 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. and Perozo E. (2001) Molecular architecture of full-length KcsA. Role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117: 165-180
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 25
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., Lee A., Chen J., Cadene M., Chalt B.T. and Mackinnon R. (2002) Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417: 515-522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chalt, B.T.5    Mackinnon, R.6
  • 26
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G., Spencer R. H., Lee A. T., Barclay M. T. and Rees D. C. (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282: 2220-2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 28
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White S. H. and Wimley W. C. (1999) Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28: 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 29
    • 0035795721 scopus 로고    scopus 로고
    • Amino acid distributions in integral membrane protein structures
    • Ulmschneider M. D. and. Sansom M. S. P. (2001) Amino acid distributions in integral membrane protein structures. Biochim. Biophys. Acta 1512: 1-14
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 1-14
    • Ulmschneider, M.D.1    Sansom, M.S.P.2
  • 33
    • 0037192124 scopus 로고    scopus 로고
    • Identification of protein side chains near the membrane-aqueous interface: A site-directed spin labeling study of KcsA
    • Gross A. and Hubbell W. L. (2002) Identification of protein side chains near the membrane-aqueous interface: a site-directed spin labeling study of KcsA. Biochemistry 41: 1123-1128
    • (2002) Biochemistry , vol.41 , pp. 1123-1128
    • Gross, A.1    Hubbell, W.L.2
  • 34
    • 0033543132 scopus 로고    scopus 로고
    • Structure of the KcsA potassium channel from Streptomyces lividans: A site-directed spin labeling study of the second transmembrane segment
    • Gross A., Columbus L., Hideg K., Altenbach C. and Hubbell W. L. (1999) Structure of the KcsA potassium channel from Streptomyces lividans: a site-directed spin labeling study of the second transmembrane segment. Biochemistry 38: 10324-10335
    • (1999) Biochemistry , vol.38 , pp. 10324-10335
    • Gross, A.1    Columbus, L.2    Hideg, K.3    Altenbach, C.4    Hubbell, W.L.5
  • 35
    • 0036789731 scopus 로고    scopus 로고
    • Interactions of phospholipids with the potassium channel KcsA
    • Williamson I. M., Alvis S. J., East J. M. and Lee A. G. (2002) Interactions of phospholipids with the potassium channel KcsA. Biophys. J. 83: 2026-2038
    • (2002) Biophys. J. , vol.83 , pp. 2026-2038
    • Williamson, I.M.1    Alvis, S.J.2    East, J.M.3    Lee, A.G.4
  • 36
    • 0033798841 scopus 로고    scopus 로고
    • Selectivity in lipid binding to the bacterial outer membrane protein OmpF
    • O'Keeffe A. H., East J. M. and Lee A. G. (2000) Selectivity in lipid binding to the bacterial outer membrane protein OmpF. Biophys. J. 79: 2066-2074
    • (2000) Biophys. J. , vol.79 , pp. 2066-2074
    • O'Keeffe, A.H.1    East, J.M.2    Lee, A.G.3
  • 40
    • 0031055885 scopus 로고    scopus 로고
    • Anionic phospholipids activate ATP-sensitive potassium channels
    • Fan Z. and Makielski J. C. (1997) Anionic phospholipids activate ATP-sensitive potassium channels. J. Biol. Chem. 272: 5388-5395
    • (1997) J. Biol. Chem. , vol.272 , pp. 5388-5395
    • Fan, Z.1    Makielski, J.C.2
  • 44
    • 0036016544 scopus 로고    scopus 로고
    • Structural and functional determinants of conserved lipid interaction domains of inward rectifying Kir6.2 channels
    • Cukras C. A., Jeliazkova I. and Nichols C. G. (2002) Structural and functional determinants of conserved lipid interaction domains of inward rectifying Kir6.2 channels. J. Gen. Physiol. 119: 581-591
    • (2002) J. Gen. Physiol. , vol.119 , pp. 581-591
    • Cukras, C.A.1    Jeliazkova, I.2    Nichols, C.G.3
  • 47
    • 0037040875 scopus 로고    scopus 로고
    • Anionic phospholipids regulate native and expressed epithelial sodium channel (ENaC)
    • Ma H. P., Saxena S. and Warnock D. G. (2002) Anionic phospholipids regulate native and expressed epithelial sodium channel (ENaC). J. Biol. Chem. 277: 7641-7644
    • (2002) J. Biol. Chem. , vol.277 , pp. 7641-7644
    • Ma, H.P.1    Saxena, S.2    Warnock, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.