메뉴 건너뛰기




Volumn 18, Issue 1, 2011, Pages 35-42

Mapping the sequence of conformational changes underlying selectivity filter gating in the Kv 11.1 potassium channel

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; POTASSIUM CHANNEL HERG; POTASSIUM ION; SODIUM ION;

EID: 78650973241     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1966     Document Type: Article
Times cited : (48)

References (55)
  • 1
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280, 69-77 (1998).
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 2
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen, G. The voltage-gated potassium channels and their relatives. Nature 419, 35-42 (2002).
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 3
    • 17044400911 scopus 로고    scopus 로고
    • A gate in the selectivity flter of potassium channels
    • Bernèche, S. & Roux, B. A gate in the selectivity flter of potassium channels. Structure 13, 591-600 (2005).
    • (2005) Structure , vol.13 , pp. 591-600
    • Bernèche, S.1    Roux, B.2
  • 4
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman, K. & Kern, D. Dynamic personalities of proteins. Nature 450, 964-972 (2007).
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 5
    • 77953714921 scopus 로고    scopus 로고
    • Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
    • Clarke, O.B. et al. Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell 141, 1018-1029 (2010).
    • (2010) Cell , vol.141 , pp. 1018-1029
    • Clarke, O.B.1
  • 8
    • 47749083052 scopus 로고    scopus 로고
    • From the frst protein structures to our current knowledge of protein folding: Delights and scepticisms
    • Fersht, A.R. From the frst protein structures to our current knowledge of protein folding: delights and scepticisms. Nat. Rev. Mol. Cell Biol. 9, 650-654 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 650-654
    • Fersht, A.R.1
  • 9
    • 0022443598 scopus 로고
    • Quantitative analysis of structure-activity relationships in engineered proteins by linear free-energy relationships
    • Fersht, A.R., Leatherbarrow, R.J. & Wells, T.N.C. Quantitative analysis of structure-activity relationships in engineered proteins by linear free-energy relationships. Nature 322, 284-286 (1986).
    • (1986) Nature , vol.322 , pp. 284-286
    • Fersht, A.R.1    Leatherbarrow, R.J.2    Wells, T.N.C.3
  • 10
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A.R., Matouschek, A. & Serrano, L. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-782 (1992).
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 11
    • 5144225084 scopus 로고    scopus 로고
    • Relationship of Leffer (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates
    • Fersht, A.R. Relationship of Leffer (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates. Proc. Natl. Acad. Sci. USA 101, 14338-14342 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14338-14342
    • Fersht, A.R.1
  • 12
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • Grosman, C., Zhou, M. & Auerbach, A. Mapping the conformational wave of acetylcholine receptor channel gating. Nature 403, 773-776 (2000).
    • (2000) Nature , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 13
    • 34247375206 scopus 로고    scopus 로고
    • A stepwise mechanism for acetylcholine receptor channel gating
    • Purohit, P., Mitra, A. & Auerbach, A. A stepwise mechanism for acetylcholine receptor channel gating. Nature 446, 930-933 (2007).
    • (2007) Nature , vol.446 , pp. 930-933
    • Purohit, P.1    Mitra, A.2    Auerbach, A.3
  • 14
    • 27744499937 scopus 로고    scopus 로고
    • Phi-value analysis of a linear, sequential reaction mechanism: Theory and application to ion channel gating
    • Zhou, Y., Pearson, J.E. & Auerbach, A. Phi-value analysis of a linear, sequential reaction mechanism: theory and application to ion channel gating. Biophys. J. 89, 3680-3685 (2005).
    • (2005) Biophys. J. , vol.89 , pp. 3680-3685
    • Zhou, Y.1    Pearson, J.E.2    Auerbach, A.3
  • 15
    • 33645317063 scopus 로고    scopus 로고
    • HERG potassium channels and cardiac arrhythmia
    • Sanguinetti, M.C. & Tristani-Firouzi, M. hERG potassium channels and cardiac arrhythmia. Nature 440, 463-469 (2006).
    • (2006) Nature , vol.440 , pp. 463-469
    • Sanguinetti, M.C.1    Tristani-Firouzi, M.2
  • 16
    • 54349123564 scopus 로고    scopus 로고
    • Drug binding to the inactivated state is necessary but not suffcient for high-affnity binding to human ether-a-go-go-related gene channels
    • Perrin, M.J., Kuchel, P.W., Campbell, T.J. & Vandenberg, J.I. Drug binding to the inactivated state is necessary but not suffcient for high-affnity binding to human ether-a-go-go-related gene channels. Mol. Pharmacol. 74, 1443-1452 (2008).
    • (2008) Mol. Pharmacol. , vol.74 , pp. 1443-1452
    • Perrin, M.J.1    Kuchel, P.W.2    Campbell, T.J.3    Vandenberg, J.I.4
  • 17
    • 0030025308 scopus 로고    scopus 로고
    • The inward rectifcation mechanism of the HERG cardiac potassium channel
    • Smith, P.L., Baukrowitz, T. & Yellen, G. The inward rectifcation mechanism of the HERG cardiac potassium channel. Nature 379, 833-836 (1996).
    • (1996) Nature , vol.379 , pp. 833-836
    • Smith, P.L.1    Baukrowitz, T.2    Yellen, G.3
  • 19
    • 59449093463 scopus 로고    scopus 로고
    • + channel
    • + channel. J. Biol. Chem. 284, 1000-1008 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 1000-1008
    • Ju, P.1
  • 20
    • 0036845677 scopus 로고    scopus 로고
    • Structural and functional role of the extracellular s5-p linker in the HERG potassium channel
    • Liu, J., Zhang, M., Jiang, M. & Tseng, G.N. Structural and functional role of the extracellular s5-p linker in the HERG potassium channel. J. Gen. Physiol. 120, 723-737 (2002).
    • (2002) J. Gen. Physiol. , vol.120 , pp. 723-737
    • Liu, J.1    Zhang, M.2    Jiang, M.3    Tseng, G.N.4
  • 21
    • 14844318017 scopus 로고    scopus 로고
    • Regional specifcity of human ether-a-go-go-related gene channel activation and inactivation gating
    • Piper, D.R., Hinz, W.A., Tallurri, C.K., Sanguinetti, M.C. & Tristani-Firouzi, M. Regional specifcity of human ether-a-go-go-related gene channel activation and inactivation gating. J. Biol. Chem. 280, 7206-7217 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 7206-7217
    • Piper, D.R.1    Hinz, W.A.2    Tallurri, C.K.3    Sanguinetti, M.C.4    Tristani-Firouzi, M.5
  • 22
    • 0142180103 scopus 로고    scopus 로고
    • + channel S5P extracellular linker: Role of an amphipathic alpha-helix in C-type inactivation
    • + channel S5P extracellular linker: role of an amphipathic alpha-helix in C-type inactivation. J. Biol. Chem. 278, 42136-42148 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 42136-42148
    • Torres, A.M.1
  • 23
    • 0032523746 scopus 로고    scopus 로고
    • + channels expressed in Xenopus oocytes reduces rectifcation by shifting the voltage dependence of inactivation
    • + channels expressed in Xenopus oocytes reduces rectifcation by shifting the voltage dependence of inactivation. J. Physiol. (Lond.) 509, 129-137 (1998).
    • (1998) J. Physiol. (Lond.) , vol.509 , pp. 129-137
    • Zou, A.1    Xu, Q.P.2    Sanguinetti, M.C.3
  • 24
    • 0029002969 scopus 로고
    • A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel
    • Sanguinetti, M.C., Jiang, C., Curran, M.E. & Keating, M.T. A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel. Cell 81, 299-307 (1995).
    • (1995) Cell , vol.81 , pp. 299-307
    • Sanguinetti, M.C.1    Jiang, C.2    Curran, M.E.3    Keating, M.T.4
  • 25
    • 0030819954 scopus 로고    scopus 로고
    • A quantitative analysis of the activation and inactivation kinetics of HERG expressed in Xenopus oocytes
    • Wang, S., Liu, S., Morales, M.J., Strauss, H.C. & Rasmusson, R.L. A quantitative analysis of the activation and inactivation kinetics of HERG expressed in Xenopus oocytes. J. Physiol. (Lond.) 502, 45-60 (1997).
    • (1997) J. Physiol. (Lond.) , vol.502 , pp. 45-60
    • Wang, S.1    Liu, S.2    Morales, M.J.3    Strauss, H.C.4    Rasmusson, R.L.5
  • 27
    • 33745662630 scopus 로고    scopus 로고
    • + permeation and block of hERG potassium channels
    • + permeation and block of hERG potassium channels. J. Gen. Physiol. 128, 55-71 (2006).
    • (2006) J. Gen. Physiol. , vol.128 , pp. 55-71
    • Gang, H.1    Zhang, S.2
  • 29
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1 Evidence for a two-state transition
    • Jackson, S.E. & Fersht, A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30, 10428-10435 (1991).
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 31
    • 35848958366 scopus 로고    scopus 로고
    • Molecular driving forces determining potassium channel slow inactivation
    • Cordero-Morales, J.F. et al. Molecular driving forces determining potassium channel slow inactivation. Nat. Struct. Mol. Biol. 14, 1062-1069 (2007).
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1062-1069
    • Cordero-Morales, J.F.1
  • 33
    • 0037197654 scopus 로고    scopus 로고
    • Structure of the transition state of gating in the acetylcholine receptor channel pore: A phi-value analysis
    • Cymes, G.D., Grosman, C. & Auerbach, A. Structure of the transition state of gating in the acetylcholine receptor channel pore: a phi-value analysis. Biochemistry 41, 5548-5555 (2002).
    • (2002) Biochemistry , vol.41 , pp. 5548-5555
    • Cymes, G.D.1    Grosman, C.2    Auerbach, A.3
  • 35
    • 0023662562 scopus 로고
    • Structure-activity relationships in engineered proteins: Analysis of use of binding energy by linear free energy relationships
    • Fersht, A.R., Leatherbarrow, R.J. & Wells, T.N. Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships. Biochemistry 26, 6030-6038 (1987).
    • (1987) Biochemistry , vol.26 , pp. 6030-6038
    • Fersht, A.R.1    Leatherbarrow, R.J.2    Wells, T.N.3
  • 36
    • 0034872511 scopus 로고    scopus 로고
    • Transition states and the meaning of Phi-values in protein folding kinetics
    • Ozkan, S.B., Bahar, I. & Dill, K.A. Transition states and the meaning of Phi-values in protein folding kinetics. Nat. Struct. Biol. 8, 765-769 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 765-769
    • Ozkan, S.B.1    Bahar, I.2    Dill, K.A.3
  • 37
    • 77954515664 scopus 로고    scopus 로고
    • + channels
    • + channels. Nature 466, 272-275 (2010).
    • (2010) Nature , vol.466 , pp. 272-275
    • Cuello, L.G.1
  • 39
    • 70349217944 scopus 로고    scopus 로고
    • +-channel: Potassium and ligand sensitivity
    • +-channel: potassium and ligand sensitivity. EMBO J. 28, 2825-2834 (2009).
    • (2009) EMBO J. , vol.28 , pp. 2825-2834
    • Ader, C.1
  • 40
    • 0028793256 scopus 로고
    • +]: A tale of two inactivation mechanisms
    • +]: a tale of two inactivation mechanisms. Neuron 15, 951-960 (1995).
    • (1995) Neuron , vol.15 , pp. 951-960
    • Baukrowitz, T.1    Yellen, G.2
  • 41
    • 33745041507 scopus 로고    scopus 로고
    • Molecular determinants of gating at the potassium-channel selectivity flter
    • Cordero-Morales, J.F. et al. Molecular determinants of gating at the potassium-channel selectivity flter. Nat. Struct. Mol. Biol. 13, 311-318 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 311-318
    • Cordero-Morales, J.F.1
  • 42
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • López-Barneo, J., Hoshi, T., Heinemann, S.H. & Aldrich, R.W. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels 1, 61-71 (1993).
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • López-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 44
    • 0032895084 scopus 로고    scopus 로고
    • Functional consequences of a decreased potassium affnity in a potassium channel pore Ion interactions and C-type inactivation
    • Ogielska, E.M. & Aldrich, R.W. Functional consequences of a decreased potassium affnity in a potassium channel pore. Ion interactions and C-type inactivation. J. Gen. Physiol. 113, 347-358 (1999).
    • (1999) J. Gen. Physiol. , vol.113 , pp. 347-358
    • Ogielska, E.M.1    Aldrich, R.W.2
  • 45
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • Jiang, Y. et al. The open pore conformation of potassium channels. Nature 417, 523-526 (2002).
    • (2002) Nature , vol.417 , pp. 523-526
    • Jiang, Y.1
  • 46
    • 36549084005 scopus 로고    scopus 로고
    • How to turn the reaction coordinate into time
    • Auerbach, A. How to turn the reaction coordinate into time. J. Gen. Physiol. 130, 543-546 (2007).
    • (2007) J. Gen. Physiol. , vol.130 , pp. 543-546
    • Auerbach, A.1
  • 47
    • 0041836223 scopus 로고    scopus 로고
    • Gating currents associated with intramembrane charge displacement in HERG potassium channels
    • Piper, D.R., Varghese, A., Sanguinetti, M.C. & Tristani-Firouzi, M. Gating currents associated with intramembrane charge displacement in HERG potassium channels. Proc. Natl. Acad. Sci. USA 100, 10534-10539 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10534-10539
    • Piper, D.R.1    Varghese, A.2    Sanguinetti, M.C.3    Tristani-Firouzi, M.4
  • 48
    • 4344686915 scopus 로고    scopus 로고
    • Molecular basis of slow activation of the human ether-a-go-go related gene potassium channel
    • Subbiah, R.N. et al. Molecular basis of slow activation of the human ether-a-go-go related gene potassium channel. J. Physiol. (Lond.) 558, 417-431 (2004).
    • (2004) J. Physiol. (Lond.) , vol.558 , pp. 417-431
    • Subbiah, R.N.1
  • 49
    • 67649789023 scopus 로고    scopus 로고
    • Aromatic residues {epsilon}Trp-55 and {delta}Trp-57 and the activation of acetylcholine receptor channels
    • Bafna, P.A., Jha, A. & Auerbach, A. Aromatic residues {epsilon}Trp-55 and {delta}Trp-57 and the activation of acetylcholine receptor channels. J. Biol. Chem. 284, 8582-8588 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 8582-8588
    • Bafna, P.A.1    Jha, A.2    Auerbach, A.3
  • 50
    • 0037126062 scopus 로고    scopus 로고
    • Position of aromatic residues in the S6 domain, not inactivation, dictates cisapride sensitivity of HERG and eag potassium channels
    • Chen, J., Seebohm, G. & Sanguinetti, M.C. Position of aromatic residues in the S6 domain, not inactivation, dictates cisapride sensitivity of HERG and eag potassium channels. Proc. Natl. Acad. Sci. USA 99, 12461-12466 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12461-12466
    • Chen, J.1    Seebohm, G.2    Sanguinetti, M.C.3
  • 51
    • 33745216690 scopus 로고    scopus 로고
    • A structural interpretation of voltage-gated potassium channel inactivation
    • Kurata, H.T. & Fedida, D. A structural interpretation of voltage-gated potassium channel inactivation. Prog. Biophys. Mol. Biol. 92, 185-208 (2006).
    • (2006) Prog. Biophys. Mol. Biol. , vol.92 , pp. 185-208
    • Kurata, H.T.1    Fedida, D.2
  • 53
    • 33750530195 scopus 로고    scopus 로고
    • Cross talk between activation and slow inactivation gates of Shaker potassium channels
    • Panyi, G. & Deutsch, C. Cross talk between activation and slow inactivation gates of Shaker potassium channels. J. Gen. Physiol. 128, 547-559 (2006).
    • (2006) J. Gen. Physiol. , vol.128 , pp. 547-559
    • Panyi, G.1    Deutsch, C.2
  • 54
    • 68149154533 scopus 로고    scopus 로고
    • Not all hERG pore domain mutations have a severe phenotype: G584S has an inactivation gating defect with mild phenotype compared to G572S, which has a dominant negative traffcking defect and a severe phenotype
    • Zhao, J.T. et al. Not all hERG pore domain mutations have a severe phenotype: G584S has an inactivation gating defect with mild phenotype compared to G572S, which has a dominant negative traffcking defect and a severe phenotype. J. Cardiovasc. Electrophysiol. 20, 923-930 (2009).
    • (2009) J. Cardiovasc. Electrophysiol. , vol.20 , pp. 923-930
    • Zhao, J.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.