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Volumn 11, Issue 11, 2003, Pages 1381-1392

Structural basis of the KcsA K+ channel and agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method

Author keywords

[No Author keywords available]

Indexed keywords

AGITOXIN 2; POTASSIUM CHANNEL; PROTEIN; PROTEIN KCSA; TOXIN; UNCLASSIFIED DRUG;

EID: 0242458492     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.10.003     Document Type: Article
Times cited : (44)

References (53)
  • 5
    • 0030745896 scopus 로고    scopus 로고
    • + channel (SKC1): Oligomeric stoichiometry and stability
    • + channel (SKC1). oligomeric stoichiometry and stability Biochemistry. 36:1997;10343-10352.
    • (1997) Biochemistry , vol.36 , pp. 10343-10352
    • Cortes, D.M.1    Perozo, E.2
  • 6
    • 8044235836 scopus 로고    scopus 로고
    • A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity
    • Cotton J., Crest M., Bouet F., Alessandri N., Gola M., Forest E., Karlsson E., Castaneda O., Harvey A.L., Vita C.et al. A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity. Eur. J. Biochem. 244:1997;192-202.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 192-202
    • Cotton, J.1    Crest, M.2    Bouet, F.3    Alessandri, N.4    Gola, M.5    Forest, E.6    Karlsson, E.7    Castaneda, O.8    Harvey, A.L.9    Vita, C.10
  • 8
    • 0026335990 scopus 로고
    • Rational design of receptor-specific variants of human growth hormone
    • Cunningham B.C., Wells J.A. Rational design of receptor-specific variants of human growth hormone. Proc. Natl. Acad. Sci. USA. 88:1991;3407-3411.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3407-3411
    • Cunningham, B.C.1    Wells, J.A.2
  • 9
    • 6544276937 scopus 로고    scopus 로고
    • On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures
    • Dauplais M., Lecoq A., Song J., Cotton J., Jamin N., Gilquin B., Roumestand C., Vita C., de Medeiros C.L., Rowan E.G.et al. On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J. Biol. Chem. 272:1997;4302-4309.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4302-4309
    • Dauplais, M.1    Lecoq, A.2    Song, J.3    Cotton, J.4    Jamin, N.5    Gilquin, B.6    Roumestand, C.7    Vita, C.8    De Medeiros, C.L.9    Rowan, E.G.10
  • 10
    • 0027466723 scopus 로고
    • Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion
    • DeBin J.A., Maggio J.E., Strichartz G.R. Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion. Am. J. Physiol. 264:1993;C361-C369.
    • (1993) Am. J. Physiol. , vol.264
    • Debin, J.A.1    Maggio, J.E.2    Strichartz, G.R.3
  • 13
    • 0036840108 scopus 로고    scopus 로고
    • Modeling the structure of agitoxin in complex with the Shaker K+ channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • Eriksson M.A., Roux B. Modeling the structure of agitoxin in complex with the Shaker K+ channel. a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles Biophys. J. 83:2002;2595-2609.
    • (2002) Biophys. J. , vol.83 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 14
    • 0024393637 scopus 로고
    • A novel potassium channel with delayed rectifier properties isolated from rat brain by expression cloning
    • Frech G.C., VanDongen A.M., Schuster G., Brown A.M., Joho R.H. A novel potassium channel with delayed rectifier properties isolated from rat brain by expression cloning. Nature. 340:1989;642-645.
    • (1989) Nature , vol.340 , pp. 642-645
    • Frech, G.C.1    Vandongen, A.M.2    Schuster, G.3    Brown, A.M.4    Joho, R.H.5
  • 17
    • 0035184148 scopus 로고    scopus 로고
    • Potassium channels: From scorpion venoms to high-resolution structure
    • Garcia M.L., Gao Y., McManus O.B., Kaczorowski G.J. Potassium channels. from scorpion venoms to high-resolution structure Toxicon. 39:2001;739-748.
    • (2001) Toxicon , vol.39 , pp. 739-748
    • Garcia, M.L.1    Gao, Y.2    Mcmanus, O.B.3    Kaczorowski, G.J.4
  • 19
    • 0028276482 scopus 로고
    • + channel: Peptide and channel residues mediating molecular recognition
    • + channel. peptide and channel residues mediating molecular recognition Neuron. 12:1994;1377-1388.
    • (1994) Neuron , vol.12 , pp. 1377-1388
    • Goldstein, S.A.1    Pheasant, D.J.2    Miller, C.3
  • 20
    • 0025195471 scopus 로고
    • 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin
    • Hanzawa H., Shimada I., Kuzuhara T., Komano H., Kohda D., Inagaki F., Natori S., Arata Y. 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin. FEBS Lett. 269:1990;413-420.
    • (1990) FEBS Lett. , vol.269 , pp. 413-420
    • Hanzawa, H.1    Shimada, I.2    Kuzuhara, T.3    Komano, H.4    Kohda, D.5    Inagaki, F.6    Natori, S.7    Arata, Y.8
  • 22
    • 0034628896 scopus 로고    scopus 로고
    • Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel
    • Imredy J.P., MacKinnon R. Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel. J. Mol. Biol. 296:2000;1283-1294.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1283-1294
    • Imredy, J.P.1    Mackinnon, R.2
  • 23
    • 0032552974 scopus 로고    scopus 로고
    • A snake toxin inhibitor of inward rectifier potassium channel ROMK1
    • Imredy J.P., Chen C., MacKinnon R. A snake toxin inhibitor of inward rectifier potassium channel ROMK1. Biochemistry. 37:1998;14867-14874.
    • (1998) Biochemistry , vol.37 , pp. 14867-14874
    • Imredy, J.P.1    Chen, C.2    Mackinnon, R.3
  • 25
    • 0036290185 scopus 로고    scopus 로고
    • Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes
    • Jayalakshmi V., Krishna N.R. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes. J. Magn. Reson. 155:2002;106-118.
    • (2002) J. Magn. Reson. , vol.155 , pp. 106-118
    • Jayalakshmi, V.1    Krishna, N.R.2
  • 26
    • 0018847395 scopus 로고
    • Snake venoms. The amino acid sequences of two Melanoleuca-type toxins
    • Joubert F.J., Taljaard N. Snake venoms. The amino acid sequences of two Melanoleuca-type toxins. Hoppe Seylers Z. Physiol. Chem. 361:1980;425-436.
    • (1980) Hoppe Seylers Z. Physiol. Chem. , vol.361 , pp. 425-436
    • Joubert, F.J.1    Taljaard, N.2
  • 27
    • 0024039181 scopus 로고
    • Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity
    • Kamb A., Tseng-Crank J., Tanouye M.A. Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity. Neuron. 1:1988;421-430.
    • (1988) Neuron , vol.1 , pp. 421-430
    • Kamb, A.1    Tseng-Crank, J.2    Tanouye, M.A.3
  • 29
    • 0029113242 scopus 로고
    • Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry
    • Krezel A.M., Kasibhatla C., Hidalgo P., MacKinnon R., Wagner G. Solution structure of the potassium channel inhibitor agitoxin 2. caliper for probing channel geometry Protein Sci. 4:1995;1478-1489.
    • (1995) Protein Sci. , vol.4 , pp. 1478-1489
    • Krezel, A.M.1    Kasibhatla, C.2    Hidalgo, P.3    Mackinnon, R.4    Wagner, G.5
  • 30
    • 0028927315 scopus 로고
    • NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels
    • Lippens G., Najib J., Wodak S.J., Tartar A. NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels. Biochemistry. 34:1995;13-21.
    • (1995) Biochemistry , vol.34 , pp. 13-21
    • Lippens, G.1    Najib, J.2    Wodak, S.J.3    Tartar, A.4
  • 31
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon R., Cohen S.L., Kuo A., Lee A., Chait B.T. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 280:1998;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
  • 32
    • 0025160126 scopus 로고
    • Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels
    • Massefski W. Jr., Redfield A.G., Hare D.R., Miller C. Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels. Science. 249:1990;521-524.
    • (1990) Science , vol.249 , pp. 521-524
    • Massefski Jr., W.1    Redfield, A.G.2    Hare, D.R.3    Miller, C.4
  • 34
    • 0008348735 scopus 로고
    • Presto (protein engineering simulator): A vectorized molecular mechanics program for biopolymers
    • Morikami K., Nakai T., Kidera A., Saito M., Nakamura H. Presto (protein engineering simulator). A vectorized molecular mechanics program for biopolymers Comput. Chem. 16:1992;243-248.
    • (1992) Comput. Chem. , vol.16 , pp. 243-248
    • Morikami, K.1    Nakai, T.2    Kidera, A.3    Saito, M.4    Nakamura, H.5
  • 36
    • 0034635351 scopus 로고    scopus 로고
    • Free energy landscapes of peptides by enhanced conformational sampling
    • Nakajima N., Higo J., Kidera A., Nakamura H. Free energy landscapes of peptides by enhanced conformational sampling. J. Mol. Biol. 296:2000;197-216.
    • (2000) J. Mol. Biol. , vol.296 , pp. 197-216
    • Nakajima, N.1    Higo, J.2    Kidera, A.3    Nakamura, H.4
  • 37
    • 0036302354 scopus 로고    scopus 로고
    • Determination of the interface of a large protein complex by transferred cross-saturation measurements
    • Nakanishi T., Miyazawa M., Sakakura M., Terasawa H., Takahashi H., Shimada I. Determination of the interface of a large protein complex by transferred cross-saturation measurements. J. Mol. Biol. 318:2002;245-249.
    • (2002) J. Mol. Biol. , vol.318 , pp. 245-249
    • Nakanishi, T.1    Miyazawa, M.2    Sakakura, M.3    Terasawa, H.4    Takahashi, H.5    Shimada, I.6
  • 39
    • 0030064382 scopus 로고    scopus 로고
    • + channel selectivity filter by mutant cycle-based structure analysis
    • + channel selectivity filter by mutant cycle-based structure analysis. Neuron. 16:1996;131-139.
    • (1996) Neuron , vol.16 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    Mackinnon, R.3
  • 40
    • 0033618255 scopus 로고    scopus 로고
    • Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin
    • Rauer H., Pennington M., Cahalan M., Chandy K.G. Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J. Biol. Chem. 274:1999;21885-21892.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21885-21892
    • Rauer, H.1    Pennington, M.2    Cahalan, M.3    Chandy, K.G.4
  • 42
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA
    • Scanlon M.J., Naranjo D., Thomas L., Alewood P.F., Lewis R.J., Craik D.J. Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA. Structure. 5:1997;1585-1597.
    • (1997) Structure , vol.5 , pp. 1585-1597
    • Scanlon, M.J.1    Naranjo, D.2    Thomas, L.3    Alewood, P.F.4    Lewis, R.J.5    Craik, D.J.6
  • 43
    • 0030273284 scopus 로고    scopus 로고
    • Ion channel associated proteins
    • Sheng M., Kim E. Ion channel associated proteins. Curr. Opin. Neurobiol. 6:1996;602-608.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 602-608
    • Sheng, M.1    Kim, E.2
  • 44
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M., Sala C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24:2001;1-29.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 46
    • 0028117321 scopus 로고
    • + channel structure from a complete functional map of the molecular surface of charybdotoxin
    • + channel structure from a complete functional map of the molecular surface of charybdotoxin. Biochemistry. 33:1994;443-450.
    • (1994) Biochemistry , vol.33 , pp. 443-450
    • Stampe, P.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 47
    • 2842522147 scopus 로고
    • Protease inhibitors as snake venom toxins
    • Strydom D.J. Protease inhibitors as snake venom toxins. Nat. New Biol. 243:1973;88-89.
    • (1973) Nat. New Biol. , vol.243 , pp. 88-89
    • Strydom, D.J.1
  • 49
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein-protein complexes
    • Takahashi H., Nakanishi T., Kami K., Arata Y., Shimada I. A novel NMR method for determining the interfaces of large protein-protein complexes. Nat. Struct. Biol. 7:2000;220-223.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 50
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilization of prey by a fish-hunting marine snail
    • Terlau H., Shon K.J., Grilley M., Stocker M., Stuhmer W., Olivera B.M. Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 381:1996;148-151.
    • (1996) Nature , vol.381 , pp. 148-151
    • Terlau, H.1    Shon, K.J.2    Grilley, M.3    Stocker, M.4    Stuhmer, W.5    Olivera, B.M.6
  • 51
    • 0029878263 scopus 로고    scopus 로고
    • Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone
    • Tudor J.E., Pallaghy P.K., Pennington M.W., Norton R.S. 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    Pennington, M.W.3    Norton, R.S.4
  • 52
    • 0032060715 scopus 로고    scopus 로고
    • On choosing a detergent for solution NMR studies of membrane proteins
    • Vinogradova O., Sonnichsen F., Sanders C.R. 2nd. On choosing a detergent for solution NMR studies of membrane proteins. J. Biomol. NMR. 11:1998;381-386.
    • (1998) J. Biomol. NMR , vol.11 , pp. 381-386
    • Vinogradova, O.1    Sonnichsen, F.2    Sanders III, C.R.3


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