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Volumn 105, Issue 33, 2008, Pages 11697-11702

Direct analysis of cooperativity in multisubunit allosteric proteins

Author keywords

Activation gate; Allosteric enzymes; Double mutant cycles; Non additivity; Voltage activated potassium channels

Indexed keywords

VOLTAGE GATED POTASSIUM CHANNEL;

EID: 50149112602     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0804104105     Document Type: Article
Times cited : (38)

References (39)
  • 1
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz MF (1989) Mechanisms of cooperativity and allosteric regulation in proteins. Q Rev Biophys 22:139-237.
    • (1989) Q Rev Biophys , vol.22 , pp. 139-237
    • Perutz, M.F.1
  • 2
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP (1965) On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 3
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland DE, Jr, Nemethy G, Filmer D (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr, D.E.1    Nemethy, G.2    Filmer, D.3
  • 4
    • 0001163089 scopus 로고
    • Kinetics of reaction control and information transfer in enzymes and nucleic acids
    • Eigen M (1967) Kinetics of reaction control and information transfer in enzymes and nucleic acids. Nobel Symp 5:333-369.
    • (1967) Nobel Symp , vol.5 , pp. 333-369
    • Eigen, M.1
  • 5
    • 0025126043 scopus 로고
    • Strategy for analyzing the co-operativity of intramolecular interactions in peptides and proteins
    • Horovitz A, Fersht AR (1990) Strategy for analyzing the co-operativity of intramolecular interactions in peptides and proteins. J Mol Biol 214:613-617.
    • (1990) J Mol Biol , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 6
    • 0026587310 scopus 로고
    • Co-operative interactions during protein folding
    • Horovitz A, Fersht AR (1992) Co-operative interactions during protein folding. J Mol Biol 224:733-740.
    • (1992) J Mol Biol , vol.224 , pp. 733-740
    • Horovitz, A.1    Fersht, A.R.2
  • 8
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla F (2000) The voltage sensor in voltage-dependent ion channels. Physiol Rev 80:555-592.
    • (2000) Physiol Rev , vol.80 , pp. 555-592
    • Bezanilla, F.1
  • 9
    • 0027971204 scopus 로고
    • Voltage gating of ion channels
    • Sigworth FJ (1994) Voltage gating of ion channels. Q Rev Biophys 27:1-40.
    • (1994) Q Rev Biophys , vol.27 , pp. 1-40
    • Sigworth, F.J.1
  • 10
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • Yellen G (1998) The moving parts of voltage-gated ion channels. Q Rev Biophys 31:239-295.
    • (1998) Q Rev Biophys , vol.31 , pp. 239-295
    • Yellen, G.1
  • 12
    • 0030906796 scopus 로고    scopus 로고
    • How does the W434F mutation block current in Shaker potassium channels?
    • Yang Y, Yan Y, Sigworth FJ (1997) How does the W434F mutation block current in Shaker potassium channels? J Gen Physiol 109:779-789.
    • (1997) J Gen Physiol , vol.109 , pp. 779-789
    • Yang, Y.1    Yan, Y.2    Sigworth, F.J.3
  • 13
  • 14
    • 12344263100 scopus 로고    scopus 로고
    • Coupling of voltage sensing to channel opening reflects intrasubunit interactions in kv channels
    • Labro AJ, Raes AL, Snyders DJ (2005) Coupling of voltage sensing to channel opening reflects intrasubunit interactions in kv channels. J Gen Physiol 125:71-80.
    • (2005) J Gen Physiol , vol.125 , pp. 71-80
    • Labro, A.J.1    Raes, A.L.2    Snyders, D.J.3
  • 15
    • 0033817708 scopus 로고    scopus 로고
    • Independence and cooperativity in rearrangements of a potassium channel voltage sensor revealed by single subunit fluorescence
    • Mannuzzu L, Isacoff EY (2000) Independence and cooperativity in rearrangements of a potassium channel voltage sensor revealed by single subunit fluorescence. J Gen Physiol 115:257-268.
    • (2000) J Gen Physiol , vol.115 , pp. 257-268
    • Mannuzzu, L.1    Isacoff, E.Y.2
  • 16
    • 0026663246 scopus 로고
    • Evidence for cooperative interactions in potassium channel gating
    • Tytgat J, Hess P (1992) Evidence for cooperative interactions in potassium channel gating. Nature 359:420-423.
    • (1992) Nature , vol.359 , pp. 420-423
    • Tytgat, J.1    Hess, P.2
  • 17
    • 0031718345 scopus 로고    scopus 로고
    • Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels
    • Zheng J, Sigworth FJ (1998) Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels J Gen Physiol 112:457-474.
    • (1998) J Gen Physiol , vol.112 , pp. 457-474
    • Zheng, J.1    Sigworth, F.J.2
  • 18
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
    • Carter PJ, Winter G, Wilkinson AJ, Fersht AR (1984) The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell 38:835-840.
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 19
    • 0028987938 scopus 로고
    • + channel pore through mutant cycles with a peptide inhibitor
    • + channel pore through mutant cycles with a peptide inhibitor. Science 268:307-310.
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2
  • 20
    • 0030322783 scopus 로고    scopus 로고
    • Double-mutant cycles: A powerful tool for analyzing protein structure and function
    • Horovitz A (1996) Double-mutant cycles: A powerful tool for analyzing protein structure and function. Fold Des 1:R121-126.
    • (1996) Fold Des , vol.1
    • Horovitz, A.1
  • 21
    • 0035923416 scopus 로고    scopus 로고
    • Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease
    • Chen J, Stites WE (2001) Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. Biochemistry 40:14012-14019.
    • (2001) Biochemistry , vol.40 , pp. 14012-14019
    • Chen, J.1    Stites, W.E.2
  • 23
    • 0026032209 scopus 로고
    • Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence
    • Papazian DM, Timpe LC, Jan YN, Jan LY (1991) Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence. Nature 349:305-310.
    • (1991) Nature , vol.349 , pp. 305-310
    • Papazian, D.M.1    Timpe, L.C.2    Jan, Y.N.3    Jan, L.Y.4
  • 24
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa NE, McCormack K, Tanouye MA, Sigworth FJ (1992) The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255:1712-1715.
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 25
    • 0031905513 scopus 로고    scopus 로고
    • Role of the S4 in cooperativity of voltage-dependent potassium channel activation
    • Smith-Maxwell CJ, Ledwell JL, Aldrich RW (1998) Role of the S4 in cooperativity of voltage-dependent potassium channel activation. J Gen Physiol 111:399-420.
    • (1998) J Gen Physiol , vol.111 , pp. 399-420
    • Smith-Maxwell, C.J.1    Ledwell, J.L.2    Aldrich, R.W.3
  • 26
    • 0031952461 scopus 로고    scopus 로고
    • Activation of Shaker potassium channels. III: An activation gating model for wild-type and V2 mutant channels
    • Schoppa NE, Sigworth FJ (1998) Activation of Shaker potassium channels. III: An activation gating model for wild-type and V2 mutant channels. J Gen Physiol 111:313-342.
    • (1998) J Gen Physiol , vol.111 , pp. 313-342
    • Schoppa, N.E.1    Sigworth, F.J.2
  • 27
    • 0028140472 scopus 로고
    • Shaker potassium channel gating. III: Evaluation of kinetic models for activation
    • Zagotta WN, Hoshi T, Aldrich RW (1994) Shaker potassium channel gating. III: Evaluation of kinetic models for activation. J Gen Physiol 103:321-362.
    • (1994) J Gen Physiol , vol.103 , pp. 321-362
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 28
    • 0032894433 scopus 로고    scopus 로고
    • Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation
    • Ledwell JL, Aldrich RW (1999) Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation. J Gen Physiol 113:389-414.
    • (1999) J Gen Physiol , vol.113 , pp. 389-414
    • Ledwell, J.L.1    Aldrich, R.W.2
  • 29
    • 0035175009 scopus 로고    scopus 로고
    • Hidden Markov model analysis of intermediate gating steps associated with the pore gate of Shaker potassium channels
    • Zheng J, Vankataramanan L, Sigworth FJ (2001) Hidden Markov model analysis of intermediate gating steps associated with the pore gate of Shaker potassium channels. J Gen Physiol 118:547-564.
    • (2001) J Gen Physiol , vol.118 , pp. 547-564
    • Zheng, J.1    Vankataramanan, L.2    Sigworth, F.J.3
  • 30
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • Jiang Y, et al. (2002) The open pore conformation of potassium channels. Nature 417:523-526.
    • (2002) Nature , vol.417 , pp. 523-526
    • Jiang, Y.1
  • 31
    • 33745041507 scopus 로고    scopus 로고
    • Molecular determinants of gating at the potassium-channel selectivity filter
    • Cordero-Morales JF, et al (2006) Molecular determinants of gating at the potassium-channel selectivity filter. Nat Struct Mol Biol 13:311-318.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 311-318
    • Cordero-Morales, J.F.1
  • 33
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280:69-77.
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 35
    • 24344432708 scopus 로고    scopus 로고
    • Investigating the putative glycine hinge in Shaker potassium channel
    • Ding S, Ingleby L, Ahern CA, Horn R (2005) Investigating the putative glycine hinge in Shaker potassium channel. J Gen Physiol 126:213-226.
    • (2005) J Gen Physiol , vol.126 , pp. 213-226
    • Ding, S.1    Ingleby, L.2    Ahern, C.A.3    Horn, R.4
  • 36
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon R (1991) Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature 350:232-235.
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 37
    • 0037013189 scopus 로고    scopus 로고
    • Hybrid tetramers of porcine liver fructose-1,6-bisphosphatase reveal multiple pathways of allosteric inhibition
    • Nelson SW, Honzatko RB, Fromm HJ (2002) Hybrid tetramers of porcine liver fructose-1,6-bisphosphatase reveal multiple pathways of allosteric inhibition. J Biol Chem 277:15539-15545.
    • (2002) J Biol Chem , vol.277 , pp. 15539-15545
    • Nelson, S.W.1    Honzatko, R.B.2    Fromm, H.J.3
  • 38
    • 0034665982 scopus 로고    scopus 로고
    • The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase
    • Sakash JB, Kantrowitz ER (2000) The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase. J Biol Chem 275:28701-28707.
    • (2000) J Biol Chem , vol.275 , pp. 28701-28707
    • Sakash, J.B.1    Kantrowitz, E.R.2


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