메뉴 건너뛰기




Volumn 77, Issue 3, 1999, Pages 1363-1373

1H-NMR and circular dichroism spectroscopic studies on changes in secondary structures of the sodium channel inactivation gate peptides as caused by the pentapeptide KIFMK

Author keywords

[No Author keywords available]

Indexed keywords

PENTAPEPTIDE; PEPTIDE; SODIUM CHANNEL; SODIUM CHANNEL AFFECTING AGENT; OLIGOPEPTIDE; SODIUM CHANNEL BLOCKING AGENT;

EID: 0032589271     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0006-3495(99)76985-7     Document Type: Article
Times cited : (11)

References (40)
  • 2
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer sepctroscopy
    • Bax, A., and D. G. Davis. 1985a. MLEV-17-based two-dimensional homonuclear magnetization transfer sepctroscopy. J. Magn. Reson. 65: 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 3
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax, A., and D. G. Davis. 1985b. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63:207-213.
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 4
    • 0000103150 scopus 로고
    • Chemical shifts in the nuclear magnetic resonance spectra of molecules containing polar groups
    • Buckingham, A. D. 1960. Chemical shifts in the nuclear magnetic resonance spectra of molecules containing polar groups. Can. J. Chem. 38:300-307.
    • (1960) Can. J. Chem. , vol.38 , pp. 300-307
    • Buckingham, A.D.1
  • 5
    • 0026490286 scopus 로고
    • Cellular and molecular biology of voltage-gated sodium channels
    • Catterall, W. A. 1992. Cellular and molecular biology of voltage-gated sodium channels. Physiol. Rev. 72:S15-S48.
    • (1992) Physiol. Rev. , vol.72
    • Catterall, W.A.1
  • 6
    • 0000456302 scopus 로고
    • Free energy perturbation calculations of charge interactions with the helix dipole
    • Daggett, V. D., P. A. Kollman, and I. D. Kuntz. 1989. Free energy perturbation calculations of charge interactions with the helix dipole. C/i/m. Scripta. 29A:205-215.
    • (1989) C/i/m. Scripta. , vol.29 A , pp. 205-215
    • Daggett, V.D.1    Kollman, P.A.2    Kuntz, I.D.3
  • 8
    • 0028363484 scopus 로고
    • Restoration of inactivation and block of open sodium channels by an inactivation gate peptide
    • Eaholtz, G., T. Scheuer, and W. A. Catterall. 1994. Restoration of inactivation and block of open sodium channels by an inactivation gate peptide. Neuron. 12:1041-1048.
    • (1994) Neuron. , vol.12 , pp. 1041-1048
    • Eaholtz, G.1    Scheuer, T.2    Catterall, W.A.3
  • 9
    • 0031931679 scopus 로고    scopus 로고
    • Kinetic analysis of block of open sodium channels by a peptide containing the isdleucine, phenylalanine, and methionine (IFM) motif from the inactivation gate
    • Eaholtz, G., W. N. Zagotta, and W. A. Catterall. 1998. Kinetic analysis of block of open sodium channels by a peptide containing the isdleucine, phenylalanine, and methionine (IFM) motif from the inactivation gate. J. Gen. Physiol. 111:75-82.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 75-82
    • Eaholtz, G.1    Zagotta, W.N.2    Catterall, W.A.3
  • 10
    • 0026530472 scopus 로고
    • Primary structure and functional expression of the human cardiac tetrodotoxin-insensitive voltage-dependent sodium channel
    • Gellens, M. E., A. L. George, Jr., L. Chen, M. Chahine, R. Horn, R. L. Barchi, and R. G. Kallen. 1992. Primary structure and functional expression of the human cardiac tetrodotoxin-insensitive voltage-dependent sodium channel. Proc. Nail. Acad. Sei. USA. 89:554-558.
    • (1992) Proc. Nail. Acad. Sei. USA. , vol.89 , pp. 554-558
    • Gellens, M.E.1    George Jr., A.L.2    Chen, L.3    Chahine, M.4    Horn, R.5    Barchi, R.L.6    Kallen, R.G.7
  • 11
    • 0026556506 scopus 로고
    • Primary structure of the adult human skeletal muscle voltage-dependent sodium channel
    • George, A. L., Jr., J. Komisarof, R. G. Kallen, and R. L. Barchi. 1992. Primary structure of the adult human skeletal muscle voltage-dependent sodium channel. Ann. Neural. 31:131-137.
    • (1992) Ann. Neural. , vol.31 , pp. 131-137
    • George Jr., A.L.1    Komisarof, J.2    Kallen, R.G.3    Barchi, R.L.4
  • 12
    • 0031455341 scopus 로고    scopus 로고
    • Competition for binding between veratridine and KIFMK: An open channel blocking peptide of the RIIA sodium channel
    • Ghatpande, A. S., and S. K. Sikdar. 1997. Competition for binding between veratridine and KIFMK: an open channel blocking peptide of the RIIA sodium channel. J. Membr. Biol. 160:177-182.
    • (1997) J. Membr. Biol. , vol.160 , pp. 177-182
    • Ghatpande, A.S.1    Sikdar, S.K.2
  • 13
    • 0029863726 scopus 로고    scopus 로고
    • Template-nucleated alanine-Iysine helices are stabilized by position-dependent interactions between the lysine side chain and the helix barrel
    • Groebke, K., P. Renold, K. Y. Tsang, T. J. Alien, K. F. McClure, and D. S. Kemp. 1996. Template-nucleated alanine-Iysine helices are stabilized by position-dependent interactions between the lysine side chain and the helix barrel. Proc. Nail. Acad. Sei. USA. 93:4025-4029.
    • (1996) Proc. Nail. Acad. Sei. USA. , vol.93 , pp. 4025-4029
    • Groebke, K.1    Renold, P.2    Tsang, K.Y.3    Alien, T.J.4    McClure, K.F.5    Kemp, D.S.6
  • 16
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop
    • Joseph, D., G. A. Petsko, and M. Karplus. 1990. Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Science. 249:1425-1428.
    • (1990) Science. , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 19
    • 0029737304 scopus 로고    scopus 로고
    • Single-channel analysis of inactivation-defective rat skeletal muscle sodium channels containing the F1304Q mutation
    • Lawrence, J. H., D. W. Orias, J. R. Baiser, H. B. NUSS, G. F. Tomaselli, B. O'Rourke, and E. Marban. 1996. Single-channel analysis of inactivation-defective rat skeletal muscle sodium channels containing the F1304Q mutation. Biophys. J. 71:1285-1294.
    • (1996) Biophys. J. , vol.71 , pp. 1285-1294
    • Lawrence, J.H.1    Orias, D.W.2    Baiser, J.R.3    Nuss, H.B.4    Tomaselli, G.F.5    O'Rourke, B.6    Marban, E.7
  • 23
    • 0029044707 scopus 로고
    • A critical role for transmembrane segment IVS6 of the sodium channel a subunit in fast inactivation
    • McPhee, J. C., D. S. Ragsdale, T. Scheuer, and W. A. Catterall. 1995. A critical role for transmembrane segment IVS6 of the sodium channel a subunit in fast inactivation. J. Biol. Cliem. 270:12025-12034.
    • (1995) J. Biol. Cliem. , vol.270 , pp. 12025-12034
    • McPhee, J.C.1    Ragsdale, D.S.2    Scheuer, T.3    Catterall, W.A.4
  • 24
    • 0031975208 scopus 로고    scopus 로고
    • A critical role for the S4-S5 intracellular loop in domain IV of the sodium channel a-subunit in fast inactivation
    • McPhee, J. C., D. S. Ragsdale, T. Scheuer, and W. A. Catterall. 1998. A critical role for the S4-S5 intracellular loop in domain IV of the sodium channel a-subunit in fast inactivation. J. Biol. Chem. 273:1121-1129.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1121-1129
    • McPhee, J.C.1    Ragsdale, D.S.2    Scheuer, T.3    Catterall, W.A.4
  • 25
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. /. Biomol. NMR. 5:14-24.
    • (1995) Biomol. NMR. , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 26
    • 0001505878 scopus 로고
    • Experimental techniques of two-dimensional correlated spectroscopy
    • Nagayama, K., A. Kumar, K. Wiithrich, and R. R. Ernst. 1980. Experimental techniques of two-dimensional correlated spectroscopy. J. Magn. Reson. 40:321-334.
    • (1980) J. Magn. Reson. , vol.40 , pp. 321-334
    • Nagayama, K.1    Kumar, A.2    Wiithrich, K.3    Ernst, R.R.4
  • 28
    • 0026439086 scopus 로고
    • Amino acid residues required for fast Na+-channel inactivation: Charge neutralizations and deletions in the III-IV linker
    • Patton, D. E., J. W. West, W. A. Catterall, and A. L. Goldin. 1992. Amino acid residues required for fast Na+-channel inactivation: charge neutralizations and deletions in the III-IV linker. Proc. Natl. Acad. Sei. USA. 89:10905-10909.
    • (1992) Proc. Natl. Acad. Sei. USA. , vol.89 , pp. 10905-10909
    • Patton, D.E.1    West, J.W.2    Catterall, W.A.3    Goldin, A.L.4
  • 30
    • 0030855929 scopus 로고    scopus 로고
    • Interaction between the sodium channel inactivation linker and domain III S4-S5
    • Smith, M. R., and A. L. Goldin. 1997. Interaction between the sodium channel inactivation linker and domain III S4-S5. Biophys. J. 73: 1885-1895.
    • (1997) Biophys. J. , vol.73 , pp. 1885-1895
    • Smith, M.R.1    Goldin, A.L.2
  • 31
    • 0001127336 scopus 로고
    • The action of local anesthetics on ion channels of excitable tissues
    • G. R. Strichartz, editor. Springer-Verlag, New York.
    • Strichartz, G. R., and J. M. Ritchie. 1987. The action of local anesthetics on ion channels of excitable tissues. In Local Anesthetics. G. R. Strichartz, editor. Springer-Verlag, New York. 21-52.
    • (1987) Local Anesthetics. , pp. 21-52
    • Strichartz, G.R.1    Ritchie, J.M.2
  • 32
    • 0029814358 scopus 로고    scopus 로고
    • Role of an S4-S5 linker in sodium channel inactivation probed by mutagenesis and a peptide blocker
    • Tang, L., R. G. Kallen, and R. Horn. 1996. Role of an S4-S5 linker in sodium channel inactivation probed by mutagenesis and a peptide blocker. J. Gen. Physiol. 108:89-104.
    • (1996) J. Gen. Physiol. , vol.108 , pp. 89-104
    • Tang, L.1    Kallen, R.G.2    Horn, R.3
  • 33
    • 0031768734 scopus 로고    scopus 로고
    • Role of hydrophobicity and solvent-mediated chargecharge interactions in stabilizing a-helices
    • Vila, J. A., D. R. Ripoli, M. E. Villegas, Y. N. Vorobjev, and H. A. Scheraga. 1998. Role of hydrophobicity and solvent-mediated chargecharge interactions in stabilizing a-helices. Biophys. J. 75:2637-2646.
    • (1998) Biophys. J. , vol.75 , pp. 2637-2646
    • Vila, J.A.1    Ripoli, D.R.2    Villegas, M.E.3    Vorobjev, Y.N.4    Scheraga, H.A.5
  • 36
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart, D. S., and B. D. Sykes. 1994. Chemical shifts as a tool for structure determination. Methods Enzymol. 239:363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 37
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., B. D. Sykes, and F. M. Richards. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 38
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., B. D. Sykes, and F. M. Richards. 1992. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1647-1651.
    • (1992) Biochemistry. , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 39
    • 0019871847 scopus 로고
    • Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution
    • Wu, C.-S. C., K. Ikeda, and J. T. Yang. 1981. Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry. 20:566-570.
    • (1981) Biochemistry. , vol.20 , pp. 566-570
    • Wu, C.-S.C.1    Ikeda, K.2    Yang, J.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.