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Volumn 3, Issue 1, 2009, Pages 39-45

Contribution of the central hydrophobic residue in the PXP motif of voltage-dependent K+ channels to S6 flexibility and gating properties

Author keywords

Gating; KV1.1; Potassium channels; S6 helix; Shaker; V404

Indexed keywords

ISOLEUCINE; PROTEIN S6; VALINE; VOLTAGE GATED POTASSIUM CHANNEL; KCNA1 PROTEIN, HUMAN; POTASSIUM; POTASSIUM CHANNEL KV1.1;

EID: 66149154316     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.3.1.7548     Document Type: Article
Times cited : (22)

References (40)
  • 3
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • DOI 10.1017/S0033583598003448
    • Yellen G. The moving parts of voltage-gated ion channels. Q Rev Biophys 1998; 3:239-295 (Pubitemid 29213771)
    • (1998) Quarterly Reviews of Biophysics , vol.31 , Issue.3 , pp. 239-295
    • Yellen, G.1
  • 4
    • 4344564963 scopus 로고    scopus 로고
    • V channel S6 helix as a molecular switch: Simulation studies
    • V channel S6 helix as a molecular switch: simulation studies. IEE Proc Nanobiotechnol 2004; 151:17-27.
    • (2004) IEE Proc Nanobiotechnol , vol.151 , pp. 17-27
    • Bright, J.N.1    Sansom, M.S.2
  • 5
    • 24944551911 scopus 로고    scopus 로고
    • Conformational dynamics of M2 helices in KirBac channels: Helix flexibility in relation to gating via molecular dynamics simulations
    • DOI 10.1021/bi0510429
    • Grottesi A, Domene C, Hall B, Sansom MS. Conformational eynamics of M2 helices in KirBac channels: Helix flexibility in relation to gating via molecular dynamics simulations. Biochemistry 2005; 44:14586-14594 (Pubitemid 41567466)
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14586-14594
    • Grottesi, A.1    Domene, C.2    Hall, B.3    Sansom, M.S.P.4
  • 7
    • 0036343993 scopus 로고    scopus 로고
    • Conformational dynamics of helix S6 from Shaker potassium channel: Simulation studies
    • DOI 10.1002/bip.10197
    • Bright JN, Shrivastava IH, Cordes FS, Sansom MS. Conformational dynamics of helix S6 from Shaker potassium channel: Simulation studies. Biopolymers 2002; 64:303-313 (Pubitemid 34886977)
    • (2002) Biopolymers , vol.64 , Issue.6 , pp. 303-313
    • Bright, J.N.1    Shrivastava, I.H.2    Cordes, F.S.3    Sansom, M.S.P.4
  • 8
  • 13
    • 0036016539 scopus 로고    scopus 로고
    • Scanning the intracellular S6 activation gate in the shaker K+ channel
    • DOI 10.1085/jgp.20028569
    • Hackos DH, Chang TH, Swartz KJ. Scanning the intracellular S6 activation gate in the shaker K+ channel. J Gen Physiol 2002; 119:521-532 (Pubitemid 34615097)
    • (2002) Journal of General Physiology , vol.119 , Issue.6 , pp. 521-531
    • Hackos, D.H.1    Chang, T.-H.2    Swartz, K.J.3
  • 16
    • 23244441222 scopus 로고    scopus 로고
    • V1.2: Structural basis of electromechanical coupling
    • V1.2: Structural basis of electromechanical coupling. Science 2005b; 309:903-908
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 20
    • 0036020149 scopus 로고    scopus 로고
    • Tail end of the S6 segment: Role in permeation in Shaker potassium channels
    • DOI 10.1085/jgp.20028611
    • Ding S, Horn R. Tail end of the s6 segment: Role in permeation in shaker potassium channels. J Gen Physiol 2002; 120:87-97. (Pubitemid 34755778)
    • (2002) Journal of General Physiology , vol.120 , Issue.1 , pp. 87-97
    • Ding, S.1    Horn, R.2
  • 21
    • 0028115778 scopus 로고
    • + channel comprises part of the pore
    • + channel comprises part of the pore. Nature 1994; 367:179-182
    • (1994) Nature , vol.367 , pp. 179-182
    • Lopez, G.A.1    Jan, Y.N.2    Jan, L.Y.3
  • 23
    • 0037214137 scopus 로고    scopus 로고
    • Protein hydrogen exchange mechanism: Local fluctuations
    • DOI 10.1110/ps.0225803
    • Maity M, Lim WK, Rumbley JN, Englander SW. Protein hydrogen exchange mechanism: Local fluctuations. Protein Sci 2003; 12:153-160 (Pubitemid 36020144)
    • (2003) Protein Science , vol.12 , Issue.1 , pp. 153-160
    • Maity, H.1    Lim, W.K.2    Rumbley, J.N.3    Englander, S.W.4
  • 24
    • 33744926664 scopus 로고    scopus 로고
    • Common mechanism of pore opening shared by five different potassium channels
    • DOI 10.1529/biophysj.105.080093
    • Shrivastava IH, Bahar I. Common mechanism of pore opening shared by five different potassium channels. Biophys J 2006; 90:3929-3940 (Pubitemid 43846111)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 3929-3940
    • Shrivastava, I.H.1    Bahar, I.2
  • 25
    • 0001774017 scopus 로고
    • Fitting and statistical analysis of single-channel records
    • Sakmann B, Neher E, eds. New York: Plenum Press
    • nd Edn. New York: Plenum Press, 1995; 483-587.
    • (1995) nd Edn. , pp. 483-587
    • Colquhoun, D.1    Sigworth, F.J.2
  • 29
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • DOI 10.1007/S008940100045
    • Lindahl E, Hess B, Van der Spoel D. GROMACS 30: A package for molecular simulation and trajectory analysis. J Mol Model 2001; 7:306-317 (Pubitemid 36153547)
    • (2001) Journal of Molecular Modeling , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 31
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger O, Edholm O, Jahnig F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidycholine at full hydration, constant pressure and constant temperature. Biophys J 1997; 72:2002-2013 (Pubitemid 27184429)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 32
    • 0031880829 scopus 로고    scopus 로고
    • Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations
    • Marrink SJ, Berger O, Tieleman P, Jähnig F. Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations. Biophys J 1998; 74:931-943 (Pubitemid 28345286)
    • (1998) Biophysical Journal , vol.74 , Issue.2 I , pp. 931-943
    • Marrink, S.-J.1    Berger, O.2    Tieleman, P.3    Jahnig, F.4
  • 33
    • 0344796204 scopus 로고
    • Ion water interaction potentials derived from free-energy perturbation simulations
    • Åqvist J. Ion water interaction potentials derived from free-energy perturbation simulations. J Phys Chem 1990; 94:8021-8024
    • (1990) J Phys Chem , vol.94 , pp. 8021-8024
    • Åqvist, J.1
  • 35
    • 33846823909 scopus 로고
    • Particle mesh Ewald - an Nlog(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle mesh Ewald - an Nlog(N) method for Ewald sums in large systems. J Chem Phys 1993; 98:10089-10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 39
    • 0141792364 scopus 로고    scopus 로고
    • Allosteric changes in protein structure computed by a simple mechanical model: Hemoglobin T → R2 transition
    • DOI 10.1016/j.jmb.2003.08.027
    • Xu C, Tobi D, Bahar I. Allosteric changes in protein structure computed by a simple mechanical model: Hemoglobin T↔R2 transition. J Mol Biol 2003; 333:153-168 (Pubitemid 37153272)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.1 , pp. 153-168
    • Xu, C.1    Tobi, D.2    Bahar, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.