메뉴 건너뛰기




Volumn 101, Issue 11, 2011, Pages 2652-2660

Modeling the binding of three toxins to the voltage-gated potassium channel (Kv1.3)

Author keywords

[No Author keywords available]

Indexed keywords

CHARYBDOTOXIN; COELENTERATE VENOM; ION; KALIOTOXIN; MUTANT PROTEIN; POTASSIUM CHANNEL KV1.3; SCORPION VENOM; SHK NEUROTOXIN; TOXIN;

EID: 82955194460     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.10.029     Document Type: Article
Times cited : (50)

References (43)
  • 2
    • 34447625549 scopus 로고    scopus 로고
    • Targeting effector memory T-cells with Kv1.3 blockers
    • H. Wulff, and M. Pennington Targeting effector memory T-cells with Kv1.3 blockers Curr. Opin. Drug Discov. Devel. 10 2007 438 445
    • (2007) Curr. Opin. Drug Discov. Devel. , vol.10 , pp. 438-445
    • Wulff, H.1    Pennington, M.2
  • 4
    • 0035923519 scopus 로고    scopus 로고
    • + channels ameliorates experimental autoimmune encephalomyelitis, a model for multiple sclerosis
    • + channels ameliorates experimental autoimmune encephalomyelitis, a model for multiple sclerosis Proc. Natl. Acad. Sci. USA 98 2001 13942 13947
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13942-13947
    • Beeton, C.1    Wulff, H.2    Béraud, E.3
  • 6
    • 0026666693 scopus 로고
    • Mapping function to structure in a channel-blocking peptide: Electrostatic mutants of charybdotoxin
    • C.S. Park, and C. Miller Mapping function to structure in a channel-blocking peptide: electrostatic mutants of charybdotoxin Biochemistry 31 1992 7749 7755
    • (1992) Biochemistry , vol.31 , pp. 7749-7755
    • Park, C.S.1    Miller, C.2
  • 8
    • 0028835235 scopus 로고
    • + channel revealed by the NMR-derived structures of scorpion toxins
    • + channel revealed by the NMR-derived structures of scorpion toxins Neuron 15 1995 1169 1181
    • (1995) Neuron , vol.15 , pp. 1169-1181
    • Aiyar, J.1    Withka, J.M.2    Chandy, K.G.3
  • 9
    • 2942677403 scopus 로고    scopus 로고
    • Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel
    • K. Yu, and W. Fu H. Jiang Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel Biophys. J. 86 2004 3542 3555
    • (2004) Biophys. J. , vol.86 , pp. 3542-3555
    • Yu, K.1    Fu, W.2    Jiang, H.3
  • 10
    • 28544434796 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex
    • L. Yu, and C. Sun E.T. Olejniczak Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex Biochemistry 44 2005 15834 15841
    • (2005) Biochemistry , vol.44 , pp. 15834-15841
    • Yu, L.1    Sun, C.2    Olejniczak, E.T.3
  • 11
    • 0036151669 scopus 로고    scopus 로고
    • Conducting-state properties of the KcsA potassium channel from molecular and Brownian dynamics simulations
    • S.H. Chung, T.W. Allen, and S. Kuyucak Conducting-state properties of the KcsA potassium channel from molecular and Brownian dynamics simulations Biophys. J. 82 2002 628 645
    • (2002) Biophys. J. , vol.82 , pp. 628-645
    • Chung, S.H.1    Allen, T.W.2    Kuyucak, S.3
  • 12
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • S.F. Altschul, and T.L. Madden D.J. Lipman Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucleic Acids Res. 25 1997 3389 3402
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Lipman, D.J.3
  • 14
    • 77954895219 scopus 로고    scopus 로고
    • Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based x-ray crystallographic refinement
    • X. Chen, and Q. Wang J. Ma Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based x-ray crystallographic refinement Proc. Natl. Acad. Sci. USA 107 2010 11352 11357
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11352-11357
    • Chen, X.1    Wang, Q.2    Ma, J.3
  • 15
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 16
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T. Schwede, and J. Kopp M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Peitsch, M.C.3
  • 17
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • K. Arnold, and L. Bordoli T. Schwede The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 2006 195 201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Schwede, T.3
  • 18
    • 67649386435 scopus 로고    scopus 로고
    • Mechanism and energetics of charybdotoxin unbinding from a potassium channel from molecular dynamics simulations
    • P.C. Chen, and S. Kuyucak Mechanism and energetics of charybdotoxin unbinding from a potassium channel from molecular dynamics simulations Biophys. J. 96 2009 2577 2588
    • (2009) Biophys. J. , vol.96 , pp. 2577-2588
    • Chen, P.C.1    Kuyucak, S.2
  • 19
    • 79551667691 scopus 로고    scopus 로고
    • Comparative study of the energetics of ion permeation in Kv1.2 and KcsA potassium channels
    • T. Batu, and S. Kuyucak Comparative study of the energetics of ion permeation in Kv1.2 and KcsA potassium channels Biophys. J. 100 2011 629 636
    • (2011) Biophys. J. , vol.100 , pp. 629-636
    • Batu, T.1    Kuyucak, S.2
  • 21
    • 0036286651 scopus 로고    scopus 로고
    • Modeling diverse range of potassium channels with Brownian dynamics
    • S.H. Chung, T.W. Allen, and S. Kuyucak Modeling diverse range of potassium channels with Brownian dynamics Biophys. J. 83 2002 263 277
    • (2002) Biophys. J. , vol.83 , pp. 263-277
    • Chung, S.H.1    Allen, T.W.2    Kuyucak, S.3
  • 22
    • 35449008122 scopus 로고    scopus 로고
    • Integrating statistical pair potentials into protein complex prediction
    • J. Mintseris, and B. Pierce Z. Weng Integrating statistical pair potentials into protein complex prediction Proteins 69 2007 511 520
    • (2007) Proteins , vol.69 , pp. 511-520
    • Mintseris, J.1    Pierce, B.2    Weng, Z.3
  • 23
    • 0031036241 scopus 로고    scopus 로고
    • Three-dimensional structure of toxin OSK1 from Orthochirus scrobiculosus scorpion venom
    • V.A. Jaravine, and D.E. Nolde A.S. Arseniev Three-dimensional structure of toxin OSK1 from Orthochirus scrobiculosus scorpion venom Biochemistry 36 1997 1223 1232
    • (1997) Biochemistry , vol.36 , pp. 1223-1232
    • Jaravine, V.A.1    Nolde, D.E.2    Arseniev, A.S.3
  • 24
    • 0029878263 scopus 로고    scopus 로고
    • Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone
    • J.E. Tudor, and P.K. Pallaghy R.S. Norton Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone Nat. Struct. Biol. 3 1996 317 320
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 317-320
    • Tudor, J.E.1    Pallaghy, P.K.2    Norton, R.S.3
  • 25
    • 33645858263 scopus 로고    scopus 로고
    • Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR
    • A. Lange, and K. Giller M. Baldus Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR Nature 440 2006 959 962
    • (2006) Nature , vol.440 , pp. 959-962
    • Lange, A.1    Giller, K.2    Baldus, M.3
  • 26
    • 0037044313 scopus 로고    scopus 로고
    • Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel, Kv1.3
    • M.D. Lanigan, and K. Kalman R.S. Norton Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel, Kv1.3 Biochemistry 41 2002 11963 11971
    • (2002) Biochemistry , vol.41 , pp. 11963-11971
    • Lanigan, M.D.1    Kalman, K.2    Norton, R.S.3
  • 28
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • S.E. Feller, and A.D. MacKerell An improved empirical potential energy function for molecular simulations of phospholipids J. Phys. Chem. B 104 2000 7510 7515
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell, A.D.2
  • 29
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • A.D. MacKerell, and D. Bashford M. Karplus All-atom empirical potential for molecular modeling and dynamics studies of proteins J. Phys. Chem. B 102 1998 3586 3616
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1    Bashford, D.2    Karplus, M.3
  • 30
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.L. Jorgensen, and J. Chandrasekhar M.L. Klein Comparison of simple potential functions for simulating liquid water J. Chem. Phys. 79 1982 926 935
    • (1982) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 31
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 23 1977 327 341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 32
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • S. Miyamoto, and P.A. Kollman SETTLE: An analytical version of the SHAKE and RATTLE algorithm for rigid water models J. Comput. Chem. 13 1992 952 962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 33
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • G.J. Martyna, D.J. Tobias, and M.L. Klein Constant pressure molecular dynamics algorithms J. Chem. Phys. 101 1994 4177 4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 34
    • 79959663208 scopus 로고    scopus 로고
    • Accurate determination of the binding free energy for KcsA-charybdotoxin complex from the potential of mean force calculations with restraints
    • P.C. Chen, and S. Kuyucak Accurate determination of the binding free energy for KcsA-charybdotoxin complex from the potential of mean force calculations with restraints Biophys. J. 100 2011 2466 2474
    • (2011) Biophys. J. , vol.100 , pp. 2466-2474
    • Chen, P.C.1    Kuyucak, S.2
  • 35
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • S. Kumar, and D. Bouzida J.M. Rosenberg The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method J. Comput. Chem. 13 1992 1011 1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Rosenberg, J.M.3
  • 36
    • 0030333470 scopus 로고    scopus 로고
    • Three-dimensional hydrogen-bond geometry and probability information from a crystal survey
    • J.E. Mills, and P.M. Dean Three-dimensional hydrogen-bond geometry and probability information from a crystal survey J. Comput. Aided Mol. Des. 10 1996 607 622
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 607-622
    • Mills, J.E.1    Dean, P.M.2
  • 37
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • S. Kumar, and R. Nussinov Close-range electrostatic interactions in proteins ChemBioChem 3 2002 604 617
    • (2002) ChemBioChem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 38
    • 0028228251 scopus 로고
    • + channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines
    • + channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines Mol. Pharmacol. 45 1994 1227 1234
    • (1994) Mol. Pharmacol. , vol.45 , pp. 1227-1234
    • Grissmer, S.1    Nguyen, A.N.2    Chandy, K.G.3
  • 40
    • 30044444119 scopus 로고    scopus 로고
    • Pharmacological profiling of Orthochirus scrobiculosus toxin 1 analogs with a trimmed N-terminal domain
    • S. Mouhat, and G. Teodorescu J.M. Sabatier Pharmacological profiling of Orthochirus scrobiculosus toxin 1 analogs with a trimmed N-terminal domain Mol. Pharmacol. 69 2006 354 362
    • (2006) Mol. Pharmacol. , vol.69 , pp. 354-362
    • Mouhat, S.1    Teodorescu, G.2    Sabatier, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.