메뉴 건너뛰기




Volumn 126, Issue 3, 2005, Pages 213-226

Investigating the putative glycine hinge in Shaker potassium channel

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GLYCINE; MUTANT PROTEIN; POTASSIUM CHANNEL BLOCKING AGENT; POTASSIUM ION; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 24344432708     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.200509287     Document Type: Article
Times cited : (77)

References (72)
  • 1
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., I. Smirnova, V. Kasho, G. Verner, H.R. Kaback, and S. Iwata. 2003. Structure and mechanism of the lactose permease of Escherichia coli. Science. 301:610-615.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 2
    • 0015142234 scopus 로고
    • Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons
    • Armstrong, C.M. 1971. Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons. J. Gen. Physiol. 58:413-437.
    • (1971) J. Gen. Physiol. , vol.58 , pp. 413-437
    • Armstrong, C.M.1
  • 3
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D.J., and J.M. Thornton. 1988. Helix geometry in proteins. J. Mol. Biol. 201:601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 5
    • 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
  • 6
    • 0037448550 scopus 로고    scopus 로고
    • The flexing/twirling helix: Exploring the flexibility about molecular hinges formed by proline and glycine motifs in transmembrane helices
    • Bright, J.N., and M.S.P. Sansom. 2003. The flexing/twirling helix: exploring the flexibility about molecular hinges formed by proline and glycine motifs in transmembrane helices. J. Phys. Chem. B. 107:627-636.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 627-636
    • Bright, J.N.1    Sansom, M.S.P.2
  • 7
    • 0036343993 scopus 로고    scopus 로고
    • Conformational dynamics of helix S6 from Shaker potassium channel: Simulation studies
    • Bright, J.N., I.H. Shrivastava, F.S. Cordes, and M.S.P. Sansom. 2002. Conformational dynamics of helix S6 from Shaker potassium channel: simulation studies. Biopolymers. 64:303-313.
    • (2002) Biopolymers , vol.64 , pp. 303-313
    • Bright, J.N.1    Shrivastava, I.H.2    Cordes, F.S.3    Sansom, M.S.P.4
  • 8
    • 0025804130 scopus 로고
    • Large differences in the helix propensities of alanine and glycine
    • Chakrabartty, A., J.A. Schellman, and R.L. Baldwin. 1991. Large differences in the helix propensities of alanine and glycine. Nature. 351:586-588.
    • (1991) Nature , vol.351 , pp. 586-588
    • Chakrabartty, A.1    Schellman, J.A.2    Baldwin, R.L.3
  • 9
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P.Y., and G.D. Fasman. 1974. Prediction of protein conformation. Biochemistry. 13:222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 10
    • 0036430199 scopus 로고    scopus 로고
    • Proline-induced distortions of transmembrane helices
    • Cordes, F.S., J.N. Bright, and M.S. Sansom. 2002. Proline-induced distortions of transmembrane helices. J. Mol. Biol. 323:951-960.
    • (2002) J. Mol. Biol. , vol.323 , pp. 951-960
    • Cordes, F.S.1    Bright, J.N.2    Sansom, M.S.3
  • 11
    • 0037167609 scopus 로고    scopus 로고
    • Glycosylation affects the rate of traffic of the Shaker potassium channel through the secretory pathway
    • De Souza, N.F., and S.M. Simon. 2002. Glycosylation affects the rate of traffic of the Shaker potassium channel through the secretory pathway. Biochemistry. 41:11351-11361.
    • (2002) Biochemistry , vol.41 , pp. 11351-11361
    • De Souza, N.F.1    Simon, S.M.2
  • 12
    • 0036240798 scopus 로고    scopus 로고
    • Putting the beta-breaks on membrane protein misfolding
    • Deber, C.M., and A.G. Therien. 2002. Putting the beta-breaks on membrane protein misfolding. Nat. Struct. Biol. 9:318-319.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 318-319
    • Deber, C.M.1    Therien, A.G.2
  • 15
    • 0036020149 scopus 로고    scopus 로고
    • Tail end of the S6 segment: Role in permeation in Shaker potassium channels
    • Ding, S., and R. Horn. 2002. Tail end of the S6 segment: role in permeation in Shaker potassium channels. J. Gen. Physiol. 120:87-97.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 87-97
    • Ding, S.1    Horn, R.2
  • 16
    • 0037214636 scopus 로고    scopus 로고
    • Effect of S6 tail mutations on charge movement in Shaker potassium channels
    • Ding, S., and R. Horn. 2003. Effect of S6 tail mutations on charge movement in Shaker potassium channels. Biophys. J. 84:295-305.
    • (2003) Biophys. J. , vol.84 , pp. 295-305
    • Ding, S.1    Horn, R.2
  • 17
    • 23244432676 scopus 로고    scopus 로고
    • Modeling of an ion channel in its open conformation
    • Domene, C., D. A. Doyle, and C. Venien-Bryan. 2005. Modeling of an ion channel in its open conformation. Biophys. J. 89:L01-L03.
    • (2005) Biophys. J. , vol.89
    • Domene, C.1    Doyle, D.A.2    Venien-Bryan, C.3
  • 20
    • 0032718889 scopus 로고    scopus 로고
    • Glycine insertion in the hinge region of lactose repressor protein alters DNA binding
    • Falcon, C.M., and K.S. Matthews. 1999. Glycine insertion in the hinge region of lactose repressor protein alters DNA binding. J. Biol. Chem. 274:30849-30857.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30849-30857
    • Falcon, C.M.1    Matthews, K.S.2
  • 21
    • 0027945446 scopus 로고
    • Molecular tuning of ion binding to calcium signaling proteins
    • Falke, J.J., S.K. Drake, A.L. Hazard, and O.B. Peersen. 1994. Molecular tuning of ion binding to calcium signaling proteins. Q. Rev. Biophys. 27:219-290.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 219-290
    • Falke, J.J.1    Drake, S.K.2    Hazard, A.L.3    Peersen, O.B.4
  • 22
    • 0034977038 scopus 로고    scopus 로고
    • Conformational changes in S6 coupled to the opening of cyclic-nucleotide gated channels
    • Flynn, G.E., and W.N. Zagotta. 2001. Conformational changes in S6 coupled to the opening of cyclic-nucleotide gated channels. Neuron. 30:689-698.
    • (2001) Neuron , vol.30 , pp. 689-698
    • Flynn, G.E.1    Zagotta, W.N.2
  • 23
    • 0032189949 scopus 로고    scopus 로고
    • Importance of a flexible hinge near the motor domain in kinesin-driven motility
    • Grummt, M., G. Woehlke, U. Henningsen, S. Fuchs, M. Schleicher, and M. Schliwa. 1998. Importance of a flexible hinge near the motor domain in kinesin-driven motility. EMBO J. 17:5536-5542.
    • (1998) EMBO J. , vol.17 , pp. 5536-5542
    • Grummt, M.1    Woehlke, G.2    Henningsen, U.3    Fuchs, S.4    Schleicher, M.5    Schliwa, M.6
  • 26
    • 0032168179 scopus 로고    scopus 로고
    • + channel can be trapped in the open state by an intersubunit metal bridge
    • + channel can be trapped in the open state by an intersubunit metal bridge. Neuron. 21:617-621.
    • (1998) Neuron , vol.21 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 27
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., W.N. Zagotta, and R.W. Aldrich. 1990. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 250:533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 28
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: Role of glycine in transmembrane helix association
    • Javadpour, M.M., M. Eilers, M. Groesbeek, and S.O. Smith. 1999. Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys. J. 77:1609-1618.
    • (1999) Biophys. J. , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 29
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J.Y. Chen, M. Cadene, B.T. Chait, and R. MacKinnon. 2002a. 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.Y.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 33
    • 0035974844 scopus 로고    scopus 로고
    • Rotational movement during cyclic nucleotide-gated channel opening
    • Johnson, J.P., Jr., and W.N. Zagotta. 2001. Rotational movement during cyclic nucleotide-gated channel opening. Nature. 412:917-921.
    • (2001) Nature , vol.412 , pp. 917-921
    • Johnson Jr., J.P.1    Zagotta, W.N.2
  • 34
    • 0037387189 scopus 로고    scopus 로고
    • Potassium channel gating observed with site-directed mass tagging
    • Kelly, B.L., and A. Gross. 2003. Potassium channel gating observed with site-directed mass tagging. Nat. Struct. Biol. 10:280-284.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 280-284
    • Kelly, B.L.1    Gross, A.2
  • 35
    • 0031897384 scopus 로고    scopus 로고
    • + at the potassium channel selectivity filter
    • + at the potassium channel selectivity filter. Biophys. J. 74:1840-1849.
    • (1998) Biophys. J. , vol.74 , pp. 1840-1849
    • Kiss, L.1    Korn, S.J.2
  • 36
    • 0032907373 scopus 로고    scopus 로고
    • Contribution of the selectivity filter to inactivation in potassium channels
    • Kiss, L., J. LoTurco, and S.J. Korn. 1999. Contribution of the selectivity filter to inactivation in potassium channels. Biophys. J. 76:253-263.
    • (1999) Biophys. J. , vol.76 , pp. 253-263
    • Kiss, L.1    LoTurco, J.2    Korn, S.J.3
  • 39
    • 0346118860 scopus 로고    scopus 로고
    • Gating of Shaker-type channels requires the flexibility of S6 caused by prolines
    • Labro, A.J., A.L. Raes, I. Bellens, N. Ottschytsch, and D.J. Snyders. 2003. Gating of Shaker-type channels requires the flexibility of S6 caused by prolines. J. Biol. Chem. 278:50724-50731.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50724-50731
    • Labro, A.J.1    Raes, A.L.2    Bellens, I.3    Ottschytsch, N.4    Snyders, D.J.5
  • 40
    • 0028086531 scopus 로고
    • Specificty and promiscuity in membrane helix interactions
    • Lemmon, M.A., and D.M. Engelman. 1994. Specificty and promiscuity in membrane helix interactions. Q. Rev. Biophys. 27:157-218.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 41
    • 0035023528 scopus 로고    scopus 로고
    • Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels
    • Li-Smerin, Y., and K.J. Swartz. 2001. Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels. J. Gen. Physiol. 117:205-217.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 205-217
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 42
    • 0026760920 scopus 로고
    • Glycine and beta-branched residues support and modulate peptide helicity in membrane environonments
    • Li, S.C., and C.M. Deber. 1992. Glycine and beta-branched residues support and modulate peptide helicity in membrane environon-ments. FEBS Lett. 311:217-220.
    • (1992) FEBS Lett. , vol.311 , pp. 217-220
    • Li, S.C.1    Deber, C.M.2
  • 43
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • Liu, Y.S.A., P. Sompornpisut, and E. Perozo. 2001. Structure of the KcsA channel intracellular gate in the open state. Nat. Struct. Biol. 8:883-887.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 883-887
    • Liu, Y.S.A.1    Sompornpisut, P.2    Perozo, E.3
  • 44
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur, M.W., and J.M. Thornton. 1991. Influence of proline residues on protein conformation. J. Mol. Biol. 218:397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 46
    • 0017421326 scopus 로고
    • Conductance fluctuations and ionic pores in membranes
    • Neher, E., and C.F. Stevens. 1977. Conductance fluctuations and ionic pores in membranes. Annu. Rev. Biophys. Bioeng. 6:345-381.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 345-381
    • Neher, E.1    Stevens, C.F.2
  • 47
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K.T., and W.F. DeGrado. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250:646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 51
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W.P., and D.M. Engelman. 2000. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296:911-919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 52
    • 0028175781 scopus 로고
    • Glycosylation of Shaker potassium channel protein in insect cell culture and in Xenopus oocytes
    • Santacruz-Toloza, L., Y. Huang, S.A. John, and D.M. Papazian. 1994. Glycosylation of Shaker potassium channel protein in insect cell culture and in Xenopus oocytes. Biochemistry. 33:5607-5613.
    • (1994) Biochemistry , vol.33 , pp. 5607-5613
    • Santacruz-Toloza, L.1    Huang, Y.2    John, S.A.3    Papazian, D.M.4
  • 54
    • 0026516310 scopus 로고
    • Effect of alanine versus glycine in α-helices on protein stability
    • Serrano, L., J.-L. Neira, J. Sancho, and A.R. Fersht. 1992. Effect of alanine versus glycine in α-helices on protein stability. Nature. 356:453-455.
    • (1992) Nature , vol.356 , pp. 453-455
    • Serrano, L.1    Neira, J.-L.2    Sancho, J.3    Fersht, A.R.4
  • 59
    • 0242498592 scopus 로고    scopus 로고
    • Constitutive activation of the Shaker Kv channel
    • Sukhareva, M., D.H. Hackos, and K. Swartz. 2003. Constitutive activation of the Shaker Kv channel. J. Gen. Physiol. 122:541-556.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 541-556
    • Sukhareva, M.1    Hackos, D.H.2    Swartz, K.3
  • 60
    • 0035427377 scopus 로고    scopus 로고
    • Proline-induced hinges in transmembrane helices: Possible roles in ion channel gating
    • Tieleman, D.P., I.H. Shrivastava, M.R. Ulmschneider, and M.S. Sansom. 2001. Proline-induced hinges in transmembrane helices: possible roles in ion channel gating. Proteins. 44:63-72.
    • (2001) Proteins , vol.44 , pp. 63-72
    • Tieleman, D.P.1    Shrivastava, I.H.2    Ulmschneider, M.R.3    Sansom, M.S.4
  • 61
    • 4444261061 scopus 로고    scopus 로고
    • + channel by lateral forces applied to the C-termini of inner helices
    • + channel by lateral forces applied to the C-termini of inner helices. Biophys. J. 87:1526-1536.
    • (2004) Biophys. J. , vol.87 , pp. 1526-1536
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 62
    • 0025782832 scopus 로고
    • Proline kinks in transmembrane α-helices
    • Von Heijne, G. 1991. Proline kinks in transmembrane α-helices. J. Mol. Biol. 218:499-503.
    • (1991) J. Mol. Biol. , vol.218 , pp. 499-503
    • Von Heijne, G.1
  • 65
    • 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
  • 66
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen, G. 2002. The voltage-gated potassium channels and their relatives. Nature. 419:35-42.
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 68
    • 0025996871 scopus 로고
    • Proline in α-helix: Stability and conformation studied by dynamics simulation
    • Yun, R.H., A. Anderson, and J. Hermans. 1991. Proline in α-helix: stability and conformation studied by dynamics simulation. Proteins Struct. Funct. Genet. 10:219-228.
    • (1991) Proteins Struct. Funct. Genet. , vol.10 , pp. 219-228
    • Yun, R.H.1    Anderson, A.2    Hermans, J.3
  • 69
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
    • Zagotta, W.N., T. Hoshi, and R.W. Aldrich. 1990. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science. 250:568-571.
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 71
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou, M., J.H. Morais-Cabral, S. Mann, and R. MacKinnon. 2001a. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.