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Volumn 4, Issue , 2011, Pages 41-48

An in silico approach to primaquine binding to Trp756 in the external vestibule of sodium channel Nav 1.4

Author keywords

Computer docking; Homology modeling; Nav 1.4; Oocytes; Primaquine (PQ); Site directed mutagenesis; Sodium channel; Voltage clamp

Indexed keywords

ALANINE; ASPARTIC ACID; CYSTEINE; GLUTAMIC ACID; LYSINE; PRIMAQUINE; SODIUM CHANNEL NAV1.4; TRYPTOPHAN;

EID: 84864295499     PISSN: None     EISSN: 1178699X     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (36)
  • 2
    • 0034890072 scopus 로고    scopus 로고
    • Molecular architecture of the voltage-dependent Na channel: Functional evidence for a helices in the pore
    • Yamagishi T, Li RA, Hsu K, Marbán E, Tomaselli GF. Molecular architecture of the voltage-dependent Na channel: Functional evidence for a helices in the pore. J Gen Physiol. 2001;118(2):171-182
    • (2001) J Gen Physiol , vol.118 , Issue.2 , pp. 171-182
    • Yamagishi, T.1    Li, R.A.2    Hsu, K.3    Marbán, E.4    Tomaselli, G.F.5
  • 3
    • 33750532138 scopus 로고    scopus 로고
    • Atomic determinants of statedependent block of sodium channels by charged local anesthetics and benzocaine
    • Tikhonov D, Bruhova I, Zhorov BS. Atomic determinants of statedependent block of sodium channels by charged local anesthetics and benzocaine. FEBS Lett. 2006;580(26):6027-6032
    • (2006) FEBS Lett , vol.580 , Issue.26 , pp. 6027-6032
    • Tikhonov, D.1    Bruhova, I.2    Zhorov, B.S.3
  • 5
    • 0034037331 scopus 로고    scopus 로고
    • Lidocaine alters activation gating of cardiac Na channels
    • Hanck DA, Makielski JC, Sheets M. Lidocaine alters activation gating of cardiac Na channels. Pflügers Arch. 2000;439(6):814-821
    • (2000) Pflügers Arch , vol.439 , Issue.6 , pp. 814-821
    • Hanck, D.A.1    Makielski, J.C.2    Sheets, M.3
  • 6
    • 0034050454 scopus 로고    scopus 로고
    • A critical residue for isorform difference in tetrodotoxin affinity is a molecular determinant of the external access path for local anesthetics in the cardiac sodium channel
    • Sunami A, Glaaser IW, Fozzard HA. A critical residue for isorform difference in tetrodotoxin affinity is a molecular determinant of the external access path for local anesthetics in the cardiac sodium channel. Proc Natl Acad Sci U S A. 2000;97(5):2326-2331
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.5 , pp. 2326-2331
    • Sunami, A.1    Glaaser, I.W.2    Fozzard, H.A.3
  • 7
    • 23644439944 scopus 로고    scopus 로고
    • Sodium channel activators: Model of binding inside the pore and a possible mechanism of action
    • Tikhonov DB, Zhorov BS. Sodium channel activators: model of binding inside the pore and a possible mechanism of action. FEBS Lett. 2005;579(20):4207-4212
    • (2005) FEBS Lett , vol.579 , Issue.20 , pp. 4207-4212
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 8
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy server
    • Walker, John M, editor, 1st ed. New York: Humana Press
    • Gasteiger E, Hoogland C, Gattiker A, et al. Protein identification and analysis tools on the ExPASy server. In: Walker, John M, editor. The Proteomics Protocols Handbook. 1st ed. New York: Humana Press; 2005:571-607
    • (2005) The Proteomics Protocols Handbook , pp. 571-607
    • Gasteiger, E.1    Hoogland, C.2    Gattiker, A.3
  • 9
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 1983;22(12):2577-2637
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 10
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on positionspecific scoring matrices
    • Jones DT. Protein secondary structure prediction based on positionspecific scoring matrices. J Mol Biol. 1999;292(2):195-202
    • (1999) J Mol Biol , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 11
    • 0033106244 scopus 로고    scopus 로고
    • Evaluation and improvement of multiple sequence methods for protein secondary structure prediction
    • Cuff JA, Barton GJ. Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. Proteins. 1999;34(4):508-519
    • (1999) Proteins , vol.34 , Issue.4 , pp. 508-519
    • Cuff, J.A.1    Barton, G.J.2
  • 12
    • 0029996162 scopus 로고    scopus 로고
    • Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence
    • Frishman D, Argos P. Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence. Protein Eng. 1996;9(2):133-142
    • (1996) Protein Eng , vol.9 , Issue.2 , pp. 133-142
    • Frishman, D.1    Argos, P.2
  • 13
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Muñoz V, Serrano L. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers. 1997;41(5):495-509
    • (1997) Biopolymers , vol.41 , Issue.5 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 14
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanisms of a calcium-gated potassium channel
    • Jiang Y, Lee A, Chen J, Cadene M, Chait B, Mackinnon R. Crystal structure and mechanisms of a calcium-gated potassium channel. Nature. 2002;417(6888):515-522
    • (2002) Nature , vol.417 , Issue.6888 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.5    Mackinnon, R.6
  • 15
    • 84864322034 scopus 로고    scopus 로고
    • Structure prediction of proteins with very low homology: A comprehensive introduction and a case study on aminopeptidase
    • Kaplan, Stanley P, editor, New York: Nova Science Publishers
    • Scior T, Wahab A. Structure prediction of proteins with very low homology: A comprehensive introduction and a case study on aminopeptidase. In: Kaplan, Stanley P, editor. Drug Design Research Perspectives. New York: Nova Science Publishers; 2007:675-708
    • (2007) Drug Design Research Perspectives , pp. 675-708
    • Scior, T.1    Wahab, A.2
  • 16
    • 33749449880 scopus 로고    scopus 로고
    • Docking and scoring - theoretically easy, practically impossible?
    • Coupez B, Lewis RA. Docking and scoring - theoretically easy, practically impossible? Curr Med Chem. 2006;13(25):2995-3003
    • (2006) Curr Med Chem , vol.13 , Issue.25 , pp. 2995-3003
    • Coupez, B.1    Lewis, R.A.2
  • 17
    • 33746171676 scopus 로고    scopus 로고
    • Current status of virtual screening as analysed by target class
    • Stoermer MJ. Current status of virtual screening as analysed by target class. Med Chem. 2006;2(1):89-112
    • (2006) Med Chem , vol.2 , Issue.1 , pp. 89-112
    • Stoermer, M.J.1
  • 18
    • 0038169950 scopus 로고    scopus 로고
    • Ligand binding: Functional site location, similarity and docking
    • Campbell S, Gold N, Jackson R, Westhead DR. Ligand binding: functional site location, similarity and docking. Curr Opin Struct Biol. 2003;13(3):389-395
    • (2003) Curr Opin Struct Biol , vol.13 , Issue.3 , pp. 389-395
    • Campbell, S.1    Gold, N.2    Jackson, R.3    Westhead, D.R.4
  • 19
    • 0042307528 scopus 로고    scopus 로고
    • The performance of current methods in ligand-protein docking
    • McConkey BJ, Sobolev V, Edelman M. The performance of current methods in ligand-protein docking. Curr Sci. 2002;83:845-856
    • (2002) Curr Sci , vol.83 , pp. 845-856
    • McConkey, B.J.1    Sobolev, V.2    Edelman, M.3
  • 20
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris GM, Goodsell DS, Halliday RS, et al. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem. 1998;19:1639-1662
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3
  • 21
    • 0036022957 scopus 로고    scopus 로고
    • Modified AutoDock for accurate docking of protein kinase inhibitors
    • Buzko OV, Bishop AC, Shokat KM. Modified AutoDock for accurate docking of protein kinase inhibitors. J Comput Aided Mol Des. 2002;16(2):113-127
    • (2002) J Comput Aided Mol Des , vol.16 , Issue.2 , pp. 113-127
    • Buzko, O.V.1    Bishop, A.C.2    Shokat, K.M.3
  • 22
    • 0035200608 scopus 로고    scopus 로고
    • Attractive intramolecular edge-to-face aromatic interactions in flexible organic molecules
    • Jennings WB, Farrell BM, Malone JF. Attractive intramolecular edge-to-face aromatic interactions in flexible organic molecules. Arch Chem Res. 2001;34(11):885-894
    • (2001) Arch Chem Res , vol.34 , Issue.11 , pp. 885-894
    • Jennings, W.B.1    Farrell, B.M.2    Malone, J.F.3
  • 23
    • 0242417008 scopus 로고    scopus 로고
    • Interactions with aromatic rings in chemical and biological recognition
    • Meyer EA, Castellano RK, Diederich F. Interactions with aromatic rings in chemical and biological recognition. Angew Chem Int Ed Engl. 2003;42(11):1210-1250
    • (2003) Angew Chem Int Ed Engl , vol.42 , Issue.11 , pp. 1210-1250
    • Meyer, E.A.1    Castellano, R.K.2    Diederich, F.3
  • 24
    • 4043162793 scopus 로고    scopus 로고
    • VEGA-an open platform to develop chemo-bio-informatics applications, using plug-in architecture and script programming
    • Pedretti A, Villa L, Vistoli G. VEGA-an open platform to develop chemo-bio-informatics applications, using plug-in architecture and script programming. J Comput Aided Mol Des. 2004;18:167-173
    • (2004) J Comput Aided Mol Des , vol.18 , pp. 167-173
    • Pedretti, A.1    Villa, L.2    Vistoli, G.3
  • 25
    • 84986870156 scopus 로고
    • Prediction of proton magnetic resonance shifts: The dependence on hydrogen charges obtained by iterative partial equalization of orbital electronegativity
    • Gasteiger J, Marsili M. Prediction of proton magnetic resonance shifts: the dependence on hydrogen charges obtained by iterative partial equalization of orbital electronegativity. Org Magn Resonance. 1981;15:353-360
    • (1981) Org Magn Resonance , vol.15 , pp. 353-360
    • Gasteiger, J.1    Marsili, M.2
  • 27
    • 0032919699 scopus 로고    scopus 로고
    • A molecular basis for the different local ansthetic affinites of resting versus open and inactivated states of the sodium channel
    • Li HL, Galue A, Meadows L, Ragsdale DS. A molecular basis for the different local ansthetic affinites of resting versus open and inactivated states of the sodium channel. Mol Pharmacol. 1999;55(1):134-141
    • (1999) Mol Pharmacol , vol.55 , Issue.1 , pp. 134-141
    • Li, H.L.1    Galue, A.2    Meadows, L.3    Ragsdale, D.S.4
  • 28
    • 0029614785 scopus 로고
    • Cardiac sodium channels (hH1) are intrinsically more sensitive to block by lidocaine than are skeletal muscle (mu 1) channels
    • Nuss HB, Tomaselli GF, Marbán E. Cardiac sodium channels (hH1) are intrinsically more sensitive to block by lidocaine than are skeletal muscle (mu 1) channels. J Gen Physiol. 1995;106(6):1193-1209
    • (1995) J Gen Physiol , vol.106 , Issue.6 , pp. 1193-1209
    • Nuss, H.B.1    Tomaselli, G.F.2    Marbán, E.3
  • 29
    • 0028222912 scopus 로고
    • Voltage clamping of Xenopus laevis oocytes utilizing agarose-cushion electrodes
    • Schreibmayer W, Lester HA, Dascal N. Voltage clamping of Xenopus laevis oocytes utilizing agarose-cushion electrodes. Pflugers Arch. 1994;426(5):453-458
    • (1994) Pflugers Arch , vol.426 , Issue.5 , pp. 453-458
    • Schreibmayer, W.1    Lester, H.A.2    Dascal, N.3
  • 31
    • 0032935518 scopus 로고    scopus 로고
    • Inactivated state dependence of sodium channel modulation by beta-scorpion toxin
    • Tsushima RG, Borges A, Backx PH. Inactivated state dependence of sodium channel modulation by beta-scorpion toxin. Pflügers Arch. 1999;437(5):661-668
    • (1999) Pflügers Arch , vol.437 , Issue.5 , pp. 661-668
    • Tsushima, R.G.1    Borges, A.2    Backx, P.H.3
  • 32
    • 0030753096 scopus 로고    scopus 로고
    • P-loop flexibility in Na+ channel pores revealed by single- and double-cysteine replacements
    • Tsushima RG, Li RA, Backx PH. P-loop flexibility in Na+ channel pores revealed by single- and double-cysteine replacements. J Gen Physiol. 1997;110(1):59-72
    • (1997) J Gen Physiol , vol.110 , Issue.1 , pp. 59-72
    • Tsushima, R.G.1    Li, R.A.2    Backx, P.H.3
  • 33
    • 0033616812 scopus 로고    scopus 로고
    • Distinguishing surface effects of calcium ion from pore-occupancy effects in Na+ channels
    • Armstrong CM. Distinguishing surface effects of calcium ion from pore-occupancy effects in Na+ channels. Proc Natl Acad Sci U S A. 1999; 96(7): 4158-4163
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.7 , pp. 4158-4163
    • Armstrong, C.M.1
  • 34
    • 70149112082 scopus 로고    scopus 로고
    • Using lidocaine and benzocaine to link sodium channel molecular conformations to state-dependent antiarrhythmic drug affinity
    • Hanck DA, Nikitina E, McNulty M, Fozzard HA, Lipkind G, Sheets MF. Using lidocaine and benzocaine to link sodium channel molecular conformations to state-dependent antiarrhythmic drug affinity. Circ Res. 2009;105(5):492-499
    • (2009) Circ Res , vol.105 , Issue.5 , pp. 492-499
    • Hanck, D.A.1    Nikitina, E.2    McNulty, M.3    Fozzard, H.A.4    Lipkind, G.5    Sheets, M.F.6
  • 35
    • 37849001772 scopus 로고    scopus 로고
    • Electrostatic contributions of aromatic residues in the local anesthetic receptor of voltage-gated sodium channels
    • Ahern CA, Eastwood AL, Dougherty DA, Horn R. Electrostatic contributions of aromatic residues in the local anesthetic receptor of voltage-gated sodium channels. Circ Res. 2008;102(1):86-94
    • (2008) Circ Res , vol.102 , Issue.1 , pp. 86-94
    • Ahern, C.A.1    Eastwood, A.L.2    Dougherty, D.A.3    Horn, R.4
  • 36
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen EF, Goddard TD, Huang CC, et al. UCSF Chimera-a visualization system for exploratory research and analysis. J Comput Chem. 2004;25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.