메뉴 건너뛰기




Volumn 70, Issue 3, 2008, Pages 844-854

Molecular basis of inhibitory peptide maurotoxin recognizing Kv1.2 channel explored by ZDOCK and molecular dynamic simulations

Author keywords

Kv1.2 channel; Maurotoxin; MD simulations; Molecular recognition; Protein protein docking

Indexed keywords

ASPARTIC ACID; INHIBITOR PROTEIN; MAUROTOXIN; POTASSIUM CHANNEL; POTASSIUM CHANNEL KV1.2; TOXIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 38549168519     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21706     Document Type: Article
Times cited : (51)

References (44)
  • 2
    • 0033635776 scopus 로고    scopus 로고
    • Potassium channels: Molecular defects, diseases, and therapeutic opportunities
    • Shieh CC, Coghlan M, Sullivan JP, Gopalakrishnan M. Potassium channels: molecular defects, diseases, and therapeutic opportunities. Pharmacol Rev 2000;52:557-594.
    • (2000) Pharmacol Rev , vol.52 , pp. 557-594
    • Shieh, C.C.1    Coghlan, M.2    Sullivan, J.P.3    Gopalakrishnan, M.4
  • 3
    • 0028987938 scopus 로고
    • Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor
    • Hidalgo P, MacKinnon R. Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor. Science 1995;268:307-310.
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2
  • 4
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon R, Cohen SL, Kuo A, Lee A, Chait BT. Structural conservation in prokaryotic and eukaryotic potassium channels. Science 1998;280:106-109.
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 5
    • 0037435021 scopus 로고    scopus 로고
    • Functional analysis of an archaebacterial voltage-dependent K+ channel
    • Ruta V, Jiang Y, Lee A, Chen J, MacKinnon R. Functional analysis of an archaebacterial voltage-dependent K+ channel. Nature 2003;422:180-185.
    • (2003) Nature , vol.422 , pp. 180-185
    • Ruta, V.1    Jiang, Y.2    Lee, A.3    Chen, J.4    MacKinnon, R.5
  • 9
    • 0031003031 scopus 로고    scopus 로고
    • Kharrat R, Mansuelle P, Sampieri F, Crest M, Oughideni R, Van Rietschoten J, Martin-Eauclaire MF, Rochat H, El Ayeb M. Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action on potassium channels. FEBS Lett 1997;406:284-290.
    • Kharrat R, Mansuelle P, Sampieri F, Crest M, Oughideni R, Van Rietschoten J, Martin-Eauclaire MF, Rochat H, El Ayeb M. Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action on potassium channels. FEBS Lett 1997;406:284-290.
  • 11
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems F, Roumestand C, Gilquin B, Menez A, Toma F. Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science 1991;254:1521-1523.
    • (1991) Science , vol.254 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Menez, A.4    Toma, F.5
  • 12
    • 0030783712 scopus 로고    scopus 로고
    • Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels
    • Blanc E, Sabatier JM, Kharrat R, Meunier S, el Ayeb M, Van Rietschoten J, Darbon H. Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels. Proteins 1997;29:321-333.
    • (1997) Proteins , vol.29 , pp. 321-333
    • Blanc, E.1    Sabatier, J.M.2    Kharrat, R.3    Meunier, S.4    el Ayeb, M.5    Van Rietschoten, J.6    Darbon, H.7
  • 15
    • 6944247603 scopus 로고    scopus 로고
    • Mapping of maurotoxin binding sites on hKv1.2, hKv1.3, and hIKCa1 channels
    • Visan V, Fajloun Z, Sabatier JM, Grissmer S. Mapping of maurotoxin binding sites on hKv1.2, hKv1.3, and hIKCa1 channels. Mol Pharmacol 2004;66:1103-1112.
    • (2004) Mol Pharmacol , vol.66 , pp. 1103-1112
    • Visan, V.1    Fajloun, Z.2    Sabatier, J.M.3    Grissmer, S.4
  • 17
    • 14044270108 scopus 로고    scopus 로고
    • Contribution of the functional dyad of animal toxins acting on voltage-gated Kv1-type channels
    • Mouhat S, De Waard M, Sabatier JM. Contribution of the functional dyad of animal toxins acting on voltage-gated Kv1-type channels. J Pept Sci 2005;11:65-68.
    • (2005) J Pept Sci , vol.11 , pp. 65-68
    • Mouhat, S.1    De Waard, M.2    Sabatier, J.M.3
  • 18
    • 85177153632 scopus 로고    scopus 로고
    • + channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol 1994;45:1227-1234.
    • + channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol 1994;45:1227-1234.
  • 19
    • 0036840108 scopus 로고    scopus 로고
    • + channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • + channel: a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles. Biophys J 2002;83:2595-2609.
    • (2002) Biophys J , vol.83 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 20
    • 3042814574 scopus 로고    scopus 로고
    • Simulation of the interaction between ScyTx and small conductance calcium-activated potassium channel by docking and MM-PBSA
    • Wu Y, Cao Z, Yi H, Jiang D, Mao X, Liu H, Li W. Simulation of the interaction between ScyTx and small conductance calcium-activated potassium channel by docking and MM-PBSA. Biophys J 2004;87:105-112.
    • (2004) Biophys J , vol.87 , pp. 105-112
    • Wu, Y.1    Cao, Z.2    Yi, H.3    Jiang, D.4    Mao, X.5    Liu, H.6    Li, W.7
  • 21
    • 33847345552 scopus 로고    scopus 로고
    • Interaction simulation of hERG K(+) channel with its specific BeKm-1 peptide: Insights into the selectivity of molecular recognition
    • Yi H, Cao Z, Yin S, Dai C, Wu Y, Li W. Interaction simulation of hERG K(+) channel with its specific BeKm-1 peptide: insights into the selectivity of molecular recognition. J Proteome Res 2007;6:611-620.
    • (2007) J Proteome Res , vol.6 , pp. 611-620
    • Yi, H.1    Cao, Z.2    Yin, S.3    Dai, C.4    Wu, Y.5    Li, W.6
  • 23
    • 0036841675 scopus 로고    scopus 로고
    • Brownian dynamics simulations of the recognition of the scorpion toxin maurotoxin with the voltage-gated potassium ion channels
    • Fu W, Cui M, Briggs JM, Huang X, Xiong B, Zhang Y, Luo X, Shen J, Ji R, Jiang H, Chen K. Brownian dynamics simulations of the recognition of the scorpion toxin maurotoxin with the voltage-gated potassium ion channels. Biophys J 2002;83:2370-2385.
    • (2002) Biophys J , vol.83 , pp. 2370-2385
    • Fu, W.1    Cui, M.2    Briggs, J.M.3    Huang, X.4    Xiong, B.5    Zhang, Y.6    Luo, X.7    Shen, J.8    Ji, R.9    Jiang, H.10    Chen, K.11
  • 24
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen R, Li L, Weng Z. ZDOCK: an initial-stage protein-docking algorithm. Proteins 2003;52:80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 26
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 2003;31:3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 29
    • 0036302289 scopus 로고    scopus 로고
    • Brownian dynamics simulations of the recognition of the scorpion toxin P05 with the small-conductance calcium-activated potassium channels
    • Cui M, Shen J, Briggs JM, Fu W, Wu J, Zhang Y, Luo X, Chi Z, Ji R, Jiang H, Chen K. Brownian dynamics simulations of the recognition of the scorpion toxin P05 with the small-conductance calcium-activated potassium channels. J Mol Biol 2002;318:417-428.
    • (2002) J Mol Biol , vol.318 , pp. 417-428
    • Cui, M.1    Shen, J.2    Briggs, J.M.3    Fu, W.4    Wu, J.5    Zhang, Y.6    Luo, X.7    Chi, Z.8    Ji, R.9    Jiang, H.10    Chen, K.11
  • 30
    • 38549157553 scopus 로고    scopus 로고
    • Case DA, Darden TA, Cheatham TE, III, Simmerling CL, Wang J, Duke RE, Luo R, Merz KM, Wang B, Pearlman DA, Crowley M, Brozell S, Tsui V, Gohlke H, Mongan J, Hornak V, Cui G, Beroza P, Schafmeister C, Caldwell JW, Ross WS, Kollman PA. Amber 8. San Francisco: University of California; 2004.
    • Case DA, Darden TA, Cheatham TE, III, Simmerling CL, Wang J, Duke RE, Luo R, Merz KM, Wang B, Pearlman DA, Crowley M, Brozell S, Tsui V, Gohlke H, Mongan J, Hornak V, Cui G, Beroza P, Schafmeister C, Caldwell JW, Ross WS, Kollman PA. Amber 8. San Francisco: University of California; 2004.
  • 31
    • 0034701222 scopus 로고    scopus 로고
    • Molecular dynamics simulations of nucleic acids with a generalized Born solvation model
    • Case DA, Darden TA. Molecular dynamics simulations of nucleic acids with a generalized Born solvation model. J Am Chem Soc 2000;122:2489-2498.
    • (2000) J Am Chem Soc , vol.122 , pp. 2489-2498
    • Case, D.A.1    Darden, T.A.2
  • 32
    • 0001398008 scopus 로고    scopus 로고
    • How well does a RESP (restrained electrostatic potential) model do in calculating the conformational energies of organic and biological molecules?
    • Wang J, Cieplak P, Kollman PA. How well does a RESP (restrained electrostatic potential) model do in calculating the conformational energies of organic and biological molecules? J Comput Chem 2000;21:1049-1074.
    • (2000) J Comput Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 33
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation approximate Born radii
    • Qiu D, Shenkin PS, Hollinger FP, Still WC. The GB/SA continuum model for solvation. A fast analytical method for the calculation approximate Born radii. J Phys Chem 1997;101:3005-3014.
    • (1997) J Phys Chem , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Hollinger, F.P.3    Still, W.C.4
  • 34
    • 33645961330 scopus 로고    scopus 로고
    • Flexible protein-protein docking
    • Bonvin AM. Flexible protein-protein docking. Curr Opin Struct Biol 2006;16:194-200.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 194-200
    • Bonvin, A.M.1
  • 35
    • 0026666693 scopus 로고
    • Mapping function to structure in a channel-blocking peptide: Electrostatic mutants of charybdotoxin
    • Park CS, Miller C. Mapping function to structure in a channel-blocking peptide: electrostatic mutants of charybdotoxin. Biochemistry 1992;31:7749-7755.
    • (1992) Biochemistry , vol.31 , pp. 7749-7755
    • Park, C.S.1    Miller, C.2
  • 36
    • 18744371588 scopus 로고    scopus 로고
    • Molecular dynamics and protein function
    • Karplus M, Kuriyan J. Molecular dynamics and protein function. Proc Natl Acad Sci USA 2005;102:6679-6685.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6679-6685
    • Karplus, M.1    Kuriyan, J.2
  • 37
    • 0037079570 scopus 로고    scopus 로고
    • Computational alanine scanning of the 1:1 human growth hormone-receptor complex
    • Huo S, Massova I, Kollman PA. Computational alanine scanning of the 1:1 human growth hormone-receptor complex. J Comput Chem 2002;23:15-27.
    • (2002) J Comput Chem , vol.23 , pp. 15-27
    • Huo, S.1    Massova, I.2    Kollman, P.A.3
  • 38
    • 0025160126 scopus 로고
    • Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels
    • Massefski W, Jr, Redfield AG, Hare DR, Miller C. Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels. Science 1990;249:521-524.
    • (1990) Science , vol.249 , pp. 521-524
    • Massefski Jr, W.1    Redfield, A.G.2    Hare, D.R.3    Miller, C.4
  • 39
    • 0030051784 scopus 로고    scopus 로고
    • Agitoxin footprinting the shaker potassium channel pore
    • Gross A, MacKinnon R. Agitoxin footprinting the shaker potassium channel pore. Neuron 1996;16:399-406.
    • (1996) Neuron , vol.16 , pp. 399-406
    • Gross, A.1    MacKinnon, R.2
  • 42
    • 0028276482 scopus 로고
    • + channel: Peptide and channel residues mediating molecular recognition
    • + channel: peptide and channel residues mediating molecular recognition. Neuron 1994;12:1377-1388.
    • (1994) Neuron , vol.12 , pp. 1377-1388
    • Goldstein, S.A.1    Pheasant, D.J.2    Miller, C.3
  • 44
    • 18644376965 scopus 로고    scopus 로고
    • Electrostatic recognition and induced fit in the kappa-PVIIA toxin binding to Shaker potassium channel
    • Huang X, Dong F, Zhou HX. Electrostatic recognition and induced fit in the kappa-PVIIA toxin binding to Shaker potassium channel. J Am Chem Soc 2005;127:6836-6849.
    • (2005) J Am Chem Soc , vol.127 , pp. 6836-6849
    • Huang, X.1    Dong, F.2    Zhou, H.X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.