메뉴 건너뛰기




Volumn 60, Issue 3, 2005, Pages 401-411

Increasing the molecular contacts between maurotoxin and Kv1.2 channel augments ligand affinity

Author keywords

Butantoxin; Chimera toxin; K+ channels; Maurotoxin; Molecular contacts; Scorpion toxin; Toxin affinity

Indexed keywords

BUTANTOXIN; CYSTINE; MAUROTOXIN; POTASSIUM CHANNEL; POTASSIUM ION; SCORPION VENOM; UNCLASSIFIED DRUG;

EID: 23044500282     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20509     Document Type: Article
Times cited : (10)

References (38)
  • 3
    • 0034607464 scopus 로고    scopus 로고
    • Synthesis, 1H NMR structure, and activity of a three-disulfide-bridged maurotoxin analog designed to restore the consensus motif of scorpion toxins
    • Fajloun Z, Ferrat G, Carlier E, Fathallah M, Lecomte C, Sandoz G, di Luccio E, Mabrouk K, Legros C, Darbon H, and others. Synthesis, 1H NMR structure, and activity of a three-disulfide-bridged maurotoxin analog designed to restore the consensus motif of scorpion toxins. J Biol Chem 2000;275:13605-13612.
    • (2000) J Biol Chem , vol.275 , pp. 13605-13612
    • Fajloun, Z.1    Ferrat, G.2    Carlier, E.3    Fathallah, M.4    Lecomte, C.5    Sandoz, G.6    Di Luccio, E.7    Mabrouk, K.8    Legros, C.9    Darbon, H.10
  • 8
    • 0037081826 scopus 로고    scopus 로고
    • Evolution of maurotoxin conformation and blocking efficacy towards Shaker B channels during the course of folding and oxidation in vitro
    • di Luccio E, Matavel A, Opi S, Regaya I, Sandoz G, M'Barek S, Carlier E, Estéve E, Carrega L, Fajloun Z, and others. Evolution of maurotoxin conformation and blocking efficacy towards Shaker B channels during the course of folding and oxidation in vitro. Biochem J 2002;361:409-416.
    • (2002) Biochem J , vol.361 , pp. 409-416
    • Di Luccio, E.1    Matavel, A.2    Opi, S.3    Regaya, I.4    Sandoz, G.5    M'Barek, S.6    Carlier, E.7    Estéve, E.8    Carrega, L.9    Fajloun, Z.10
  • 9
  • 11
    • 0037330864 scopus 로고    scopus 로고
    • Covalent structure and some pharmacological features of native and cleaved alpha-KTx12-1, a four disulfide-bridged toxin from Tityus serrulatus venom
    • Pimenta AM, Mansuelle P, Diniz CR, Martin-Eauclaire MF. Covalent structure and some pharmacological features of native and cleaved alpha-KTx12-1, a four disulfide-bridged toxin from Tityus serrulatus venom. J Peptide Sci 2003;9:132-140.
    • (2003) J Peptide Sci , vol.9 , pp. 132-140
    • Pimenta, A.M.1    Mansuelle, P.2    Diniz, C.R.3    Martin-Eauclaire, M.F.4
  • 13
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield RB. Solid phase synthesis. Science 1986;232:341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, R.B.1
  • 14
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill OP, Marty A, Neher E, Sakmann B, Sigworth FJ. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch 1981;391:85-100.
    • (1981) Pflugers Arch , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 15
    • 0030448653 scopus 로고    scopus 로고
    • Evidence for an internal phenylalkylamine action on the voltage-gated potassium channel Kv1.3
    • Rauer H, Grissmer S. Evidence for an internal phenylalkylamine action on the voltage-gated potassium channel Kv1.3. Mol Pharmacol 1996;50:1625-1634.
    • (1996) Mol Pharmacol , vol.50 , pp. 1625-1634
    • Rauer, H.1    Grissmer, S.2
  • 16
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Res 1989;85:393-399.
    • (1989) J Magn Res , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 17
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
    • Marion D, Wüthrich, K. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem Biophys Res Commun 1983;113:967-974.
    • (1983) Biochem Biophys Res Commun , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 18
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 1992;2:661-665.
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 20
    • 0026193519 scopus 로고
    • Efficient analysis of protein 2D NMR spectra using the software package EASY
    • Eccles C, Guntert P, Billeter M, Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY. J Biomol NMR 1991;1:111-130.
    • (1991) J Biomol NMR , vol.1 , pp. 111-130
    • Eccles, C.1    Guntert, P.2    Billeter, M.3    Wüthrich, K.4
  • 21
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • Linge JP, Habeck M, Rieping W, Nilges M. ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 2003; 19:315-316.
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 24
  • 26
    • 0034212826 scopus 로고    scopus 로고
    • BiGGER: A new (soft) docking algorithm for predicting protein interactions
    • Palma PN, Krippahl L, Wampler JE, Moura JJ. BiGGER: a new (soft) docking algorithm for predicting protein interactions. Proteins 2000;39:372-384.
    • (2000) Proteins , vol.39 , pp. 372-384
    • Palma, P.N.1    Krippahl, L.2    Wampler, J.E.3    Moura, J.J.4
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 29
    • 0034237485 scopus 로고    scopus 로고
    • Molecular dynamics simulation of hen egg white lysozyme: A test of the GROMOS96 force field against nuclear magnetic resonance data
    • Stocker U, van Gunsteren WF. Molecular dynamics simulation of hen egg white lysozyme: a test of the GROMOS96 force field against nuclear magnetic resonance data. Proteins 2000;40:145-153.
    • (2000) Proteins , vol.40 , pp. 145-153
    • Stocker, U.1    Van Gunsteren, W.F.2
  • 30
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 1995;8:127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 34
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems F, Roumestand C, Gilquin B, Ménez 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    Ménez, A.4    Toma, F.5
  • 35
    • 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 Reitschoten 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 Reitschoten, J.6    Darbon, H.7
  • 36
    • 0021944965 scopus 로고
    • Circular dichroism and its empirical application to biopolymers
    • Johnson WC. Circular dichroism and its empirical application to biopolymers. Methods Biochem Anal 1985;31:61-163.
    • (1985) Methods Biochem Anal , vol.31 , pp. 61-163
    • Johnson, W.C.1
  • 38
    • 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, and others. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.