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Volumn 49, Issue 44, 2010, Pages 9480-9487

Ion binding to KcsA: Implications in ion selectivity and channel gating

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY STATE; CHANNEL GATING; CHANNEL SELECTIVITY; CONCENTRATION-DEPENDENT; DENATURATION PROCESS; INTERSUBUNIT INTERACTION; ION BINDING; ION CHANNEL; ION CONCENTRATIONS; ION SELECTIVITY; POTASSIUM CHANNELS; PROTEIN UNFOLDING; SYNERGISTIC EFFECT; THERMAL DENATURATIONS; THERMAL STABILITY; X-RAY CHANNEL;

EID: 78149323108     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101235v     Document Type: Article
Times cited : (18)

References (45)
  • 5
    • 2142758648 scopus 로고    scopus 로고
    • Ion binding affinity in the cavity of the KcsA potassium channel
    • Zhou, Y. and MacKinnon, R. (2004) Ion binding affinity in the cavity of the KcsA potassium channel Biochemistry 43, 4978-4982
    • (2004) Biochemistry , vol.43 , pp. 4978-4982
    • Zhou, Y.1    MacKinnon, R.2
  • 6
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • MacKinnon, R. (2003) Potassium channels FEBS Lett. 555, 62-65
    • (2003) FEBS Lett. , vol.555 , pp. 62-65
    • MacKinnon, R.1
  • 7
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • Gouaux, E. and MacKinnon, R. (2005) Principles of selective ion transport in channels and pumps Science 310, 1461-1465
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    MacKinnon, R.2
  • 8
    • 7244251461 scopus 로고    scopus 로고
    • Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands
    • Noskov, S. Y., Berneche, S., and Roux, B. (2004) Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands Nature 431, 830-834
    • (2004) Nature , vol.431 , pp. 830-834
    • Noskov, S.Y.1    Berneche, S.2    Roux, B.3
  • 9
    • 34250333069 scopus 로고    scopus 로고
    • + channels is due to topological control of the permeant ion's coordinated state
    • + channels is due to topological control of the permeant ion's coordinated state Proc. Natl. Acad. Sci. U.S.A. 104, 9260-9265
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9260-9265
    • Bostick, D.L.1    Iii, L.B.C.2
  • 10
    • 35348997382 scopus 로고    scopus 로고
    • The predominant role of coordination number in potassium channel selectivity
    • Thomas, M., Jayatilaka, D., and Corry, B. (2007) The predominant role of coordination number in potassium channel selectivity Biophys. J. 93, 2635-2643
    • (2007) Biophys. J. , vol.93 , pp. 2635-2643
    • Thomas, M.1    Jayatilaka, D.2    Corry, B.3
  • 11
    • 34548262701 scopus 로고    scopus 로고
    • Tuning ion coordination architectures to enable selective partitioning
    • Varma, S. and Rempe, S. B. (2007) Tuning ion coordination architectures to enable selective partitioning Biophys. J. 93, 1093-1099
    • (2007) Biophys. J. , vol.93 , pp. 1093-1099
    • Varma, S.1    Rempe, S.B.2
  • 12
    • 38049095537 scopus 로고    scopus 로고
    • + selectivity in K channels and valinomycin: Over-coordination versus cavity-size constraints
    • + selectivity in K channels and valinomycin: over-coordination versus cavity-size constraints J. Mol. Biol. 376, 13-22
    • (2008) J. Mol. Biol. , vol.376 , pp. 13-22
    • Varma, S.1    Sabo, D.2    Rempe, S.B.3
  • 13
    • 0030752535 scopus 로고    scopus 로고
    • Single channel seeks permeant ion for brief but intimate relationship
    • Yellen, G. (1997) Single channel seeks permeant ion for brief but intimate relationship J. Gen. Physiol. 110, 83-85
    • (1997) J. Gen. Physiol. , vol.110 , pp. 83-85
    • Yellen, G.1
  • 16
    • 1542297730 scopus 로고    scopus 로고
    • K channel gating by an affinity-switching selectivity filter
    • VanDongen, A. M. (2004) K channel gating by an affinity-switching selectivity filter Proc. Natl. Acad. Sci. U.S.A. 101, 3248-3252
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3248-3252
    • Vandongen, A.M.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 1642483662 scopus 로고    scopus 로고
    • Redesigning the folding energetics of a model three-helix bundle protein by site-directed mutagenesis
    • Lopes, D. H., Chapeaurouge, A., Manderson, G. A., Johansson, J. S., and Ferreira, S. T. (2004) Redesigning the folding energetics of a model three-helix bundle protein by site-directed mutagenesis J. Biol. Chem. 279, 10991-10996
    • (2004) J. Biol. Chem. , vol.279 , pp. 10991-10996
    • Lopes, D.H.1    Chapeaurouge, A.2    Manderson, G.A.3    Johansson, J.S.4    Ferreira, S.T.5
  • 23
  • 24
    • 33645502287 scopus 로고    scopus 로고
    • Thermodynamics of unfolding of an integral membrane protein in mixed micelles
    • Sehgal, P. and Otzen, D. E. (2006) Thermodynamics of unfolding of an integral membrane protein in mixed micelles Protein Sci. 15, 890-899
    • (2006) Protein Sci. , vol.15 , pp. 890-899
    • Sehgal, P.1    Otzen, D.E.2
  • 26
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant, J. M. (1987) Biochemical applications of differential scanning calorimetry Annu. Rev. Phys. Chem. 38, 463-488
    • (1987) Annu. Rev. Phys. Chem. , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 27
    • 33846622066 scopus 로고    scopus 로고
    • Ligand effects on protein thermodynamic stability
    • Sanchez-Ruiz, J. M. (2007) Ligand effects on protein thermodynamic stability Biophys. Chem. 126, 43-49
    • (2007) Biophys. Chem. , vol.126 , pp. 43-49
    • Sanchez-Ruiz, J.M.1
  • 28
    • 0002518285 scopus 로고    scopus 로고
    • Optical spectroscopy to characterize protein conformation
    • (Creighton, T. E., Ed.) 2 nd ed., IRL Press, Oxford, U.K.
    • Schmid, F. X. (1997) Optical spectroscopy to characterize protein conformation, in Protein Structure: A Practical Approach (Creighton, T. E., Ed.) 2 nd ed., pp 261-298, IRL Press, Oxford, U.K.
    • (1997) Protein Structure: A Practical Approach , pp. 261-298
    • Schmid, F.X.1    Creighton, T.E.2
  • 31
    • 0033823118 scopus 로고    scopus 로고
    • The barium site in a potassium channel by x-ray crystallography
    • Jiang, Y. and MacKinnon, R. (2000) The barium site in a potassium channel by x-ray crystallography J. Gen. Physiol. 115, 269-272
    • (2000) J. Gen. Physiol. , vol.115 , pp. 269-272
    • Jiang, Y.1    MacKinnon, R.2
  • 33
    • 0142185496 scopus 로고    scopus 로고
    • + selectivity filter: Charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates
    • + selectivity filter: charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates J. Mol. Biol. 333, 965-975
    • (2003) J. Mol. Biol. , vol.333 , pp. 965-975
    • Zhou, Y.1    MacKinnon, R.2
  • 35
    • 17044400911 scopus 로고    scopus 로고
    • A gate in the selectivity filter of potassium channels
    • Berneche, S. and Roux, B. (2005) A gate in the selectivity filter of potassium channels Structure 13, 591-600
    • (2005) Structure , vol.13 , pp. 591-600
    • Berneche, S.1    Roux, B.2
  • 37
    • 33750530193 scopus 로고    scopus 로고
    • Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction
    • Blunck, R., Cordero-Morales, J. F., Cuello, L. G., Perozo, E., and Bezanilla, F. (2006) Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction J. Gen. Physiol. 128, 569-581
    • (2006) J. Gen. Physiol. , vol.128 , pp. 569-581
    • Blunck, R.1    Cordero-Morales, J.F.2    Cuello, L.G.3    Perozo, E.4    Bezanilla, F.5
  • 38
    • 71449094441 scopus 로고    scopus 로고
    • Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore
    • Thompson, A. N., Kim, I., Panosian, T. D., Iverson, T. M., Allen, T. W., and Nimigean, C. M. (2009) Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore Nat. Struct. Mol. Biol. 16, 1317-1324
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1317-1324
    • Thompson, A.N.1    Kim, I.2    Panosian, T.D.3    Iverson, T.M.4    Allen, T.W.5    Nimigean, C.M.6
  • 39
    • 55949109148 scopus 로고    scopus 로고
    • Conformational changes in the selectivity filter of the open-state KcsA channel: An energy minimization study
    • Miloshevsky, G. V. and Jordan, P. C. (2008) Conformational changes in the selectivity filter of the open-state KcsA channel: an energy minimization study Biophys. J. 95, 3239-3251
    • (2008) Biophys. J. , vol.95 , pp. 3239-3251
    • Miloshevsky, G.V.1    Jordan, P.C.2
  • 41
    • 0035996966 scopus 로고    scopus 로고
    • K(+) versus Na(+) ions in a K channel selectivity filter: A simulation study
    • Shrivastava, I. H., Tieleman, D. P., Biggin, P. C., and Sansom, M. S. (2002) K(+) versus Na(+) ions in a K channel selectivity filter: a simulation study Biophys. J. 83, 633-645
    • (2002) Biophys. J. , vol.83 , pp. 633-645
    • Shrivastava, I.H.1    Tieleman, D.P.2    Biggin, P.C.3    Sansom, M.S.4
  • 43
    • 9744272384 scopus 로고    scopus 로고
    • Influence of C-terminal protein domains and protein-lipid interactions on tetramerization and stability of the potassium channel KcsA
    • Molina, M. L., Encinar, J. A., Barrera, F. N., Fernandez-Ballester, G., Riquelme, G., and Gonzalez-Ros, J. M. (2004) Influence of C-terminal protein domains and protein-lipid interactions on tetramerization and stability of the potassium channel KcsA Biochemistry 43, 14924-14931
    • (2004) Biochemistry , vol.43 , pp. 14924-14931
    • Molina, M.L.1    Encinar, J.A.2    Barrera, F.N.3    Fernandez-Ballester, G.4    Riquelme, G.5    Gonzalez-Ros, J.M.6
  • 44
    • 0030752535 scopus 로고    scopus 로고
    • Single channel seeks permeant ion for brief but intimate relationship
    • Yellen, G. (1997) Single channel seeks permeant ion for brief but intimate relationship J. Gen. Physiol. 110, 83-85
    • (1997) J. Gen. Physiol. , vol.110 , pp. 83-85
    • Yellen, G.1
  • 45
    • 33644686444 scopus 로고    scopus 로고
    • A structural perspective on enzymes activated by monovalent cations
    • DiCera, E. (2006) A structural perspective on enzymes activated by monovalent cations J. Biol. Chem. 281, 1305-1308
    • (2006) J. Biol. Chem. , vol.281 , pp. 1305-1308
    • Dicera, E.1


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