메뉴 건너뛰기




Volumn 123, Issue 4, 2004, Pages 455-467

Molecular Surface of Tarantula Toxins Interacting with Voltage Sensors in Kv Channels

Author keywords

Gating modifier; Scanning mutagenesis; Spider venom; Voltage activated channels

Indexed keywords

HANATOXIN; ION CHANNEL; POTASSIUM CHANNEL; SCORPION VENOM; SEA ANEMONE TOXIN; SPIDER VENOM; TARANTULA TOXIN; UNCLASSIFIED DRUG;

EID: 1842786935     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.200309005     Document Type: Article
Times cited : (94)

References (70)
  • 3
    • 0028169761 scopus 로고
    • ω-Conotoxin block of N-type calcium channels in frog and rat sympathetic neurons
    • Boland, L.M., J.A. Morrill, and B.P. Bean. 1994. ω-Conotoxin block of N-type calcium channels in frog and rat sympathetic neurons. J. Neurosci. 14:5011-5027.
    • (1994) J. Neurosci. , vol.14 , pp. 5011-5027
    • Boland, L.M.1    Morrill, J.A.2    Bean, B.P.3
  • 4
    • 0034950016 scopus 로고    scopus 로고
    • Interaction of SNX482 with domains III and IV inhibits activation gating of α(1E) (Ca(V)2.3) calcium channels
    • Bourinet, E., S.C. Stotz, R.L. Spaetgens, G. Dayanithi, J. Lemos, J. Nargeot, and G.W. Zamponi. 2001. Interaction of SNX482 with domains III and IV inhibits activation gating of α(1E) (Ca(V)2.3) calcium channels. Biophys. J. 81:79-88.
    • (2001) Biophys. J. , vol.81 , pp. 79-88
    • Bourinet, E.1    Stotz, S.C.2    Spaetgens, R.L.3    Dayanithi, G.4    Lemos, J.5    Nargeot, J.6    Zamponi, G.W.7
  • 5
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestele, S., and W.A. Catterall. 2000. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie. 82:883-892.
    • (2000) Biochimie , vol.82 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 7
    • 0029824711 scopus 로고    scopus 로고
    • The role of exposed tryptophan residues in the activity of the cardiotonic polypeptide anthopleurin B
    • Dias-Kadambi, B.L., K.A. Combs, C.L. Drum, D.A. Hanck, and K.M. Blumenthal. 1996a. The role of exposed tryptophan residues in the activity of the cardiotonic polypeptide anthopleurin B. J. Biol. Chem. 271:23828-23835.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23828-23835
    • Dias-Kadambi, B.L.1    Combs, K.A.2    Drum, C.L.3    Hanck, D.A.4    Blumenthal, K.M.5
  • 8
    • 0030010219 scopus 로고    scopus 로고
    • Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel
    • Dias-Kadambi, B.L., C.L. Drum, D.A. Hanck, and K.M. Blumenthal. 1996b. Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel. J. Biol. Chem. 271:9422-9428.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9422-9428
    • Dias-Kadambi, B.L.1    Drum, C.L.2    Hanck, D.A.3    Blumenthal, K.M.4
  • 11
    • 0028096838 scopus 로고
    • Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin
    • Ellinor, P.T., J.F. Zhang, W.A. Horne, and R.W. Tsien. 1994. Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin. Nature. 372:272-275.
    • (1994) Nature , vol.372 , pp. 272-275
    • Ellinor, P.T.1    Zhang, J.F.2    Horne, W.A.3    Tsien, R.W.4
  • 12
    • 0037490146 scopus 로고    scopus 로고
    • Determinants of inhibition of transiently expressed voltage-gated calcium channels by omega-conotoxins GVIA and MVIIA
    • Feng, Z.P., C.J. Doering, R.J. Winkfein, A.M. Beedle, J.D. Spafford, and G.W. Zamponi. 2003. Determinants of inhibition of transiently expressed voltage-gated calcium channels by omega-conotoxins GVIA and MVIIA. J. Biol. Chem. 278:20171-20178.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20171-20178
    • Feng, Z.P.1    Doering, C.J.2    Winkfein, R.J.3    Beedle, A.M.4    Spafford, J.D.5    Zamponi, G.W.6
  • 13
    • 0024393637 scopus 로고
    • A novel potassium channel with delayed rectifier properties isolated from rat brain by expression cloning
    • Frech, G.C., A.M. VanDongen, G. Schuster, A.M. Brown, and R.H. Joho. 1989. A novel potassium channel with delayed rectifier properties isolated from rat brain by expression cloning. Nature. 340:642-645.
    • (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
  • 15
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C., and P.H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 16
    • 0028885750 scopus 로고
    • Modification of inactivation in cardiac sodium channels: Ionic current studies with Anthopleurin-A toxin
    • Hanck, D.A., and M.F. Sheets. 1995. Modification of inactivation in cardiac sodium channels: ionic current studies with Anthopleurin-A toxin. J. Gen. Physiol. 106:601-616.
    • (1995) J. Gen. Physiol. , vol.106 , pp. 601-616
    • Hanck, D.A.1    Sheets, M.F.2
  • 17
    • 0033543581 scopus 로고    scopus 로고
    • Crystal structures of two alpha-like scorpion toxins: Non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel
    • He, X.L., H.M. Li, Z.H. Zeng, X.Q. Liu, M. Wang, and D.C. Wang. 1999. Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel. J. Mol. Biol. 292:125-135.
    • (1999) J. Mol. Biol. , vol.292 , pp. 125-135
    • He, X.L.1    Li, H.M.2    Zeng, Z.H.3    Liu, X.Q.4    Wang, M.5    Wang, D.C.6
  • 18
    • 0028987938 scopus 로고
    • + channel pore through mutant cycles with a peptide inhibitor
    • + channel pore through mutant cycles with a peptide inhibitor. Science. 268:307-310.
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2
  • 20
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon. 2002a. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 24
    • 0029035945 scopus 로고
    • Multiple cationic residues of anthopleurin B that determine high affinity and channel isoform discrimination
    • Khera, P.K., G.R. Benzinger, G. Lipkind, C.L. Drum, D.A. Hanck, and K.M. Blumenthal. 1995. Multiple cationic residues of anthopleurin B that determine high affinity and channel isoform discrimination. Biochemistry. 34:8533-8541.
    • (1995) Biochemistry , vol.34 , pp. 8533-8541
    • Khera, P.K.1    Benzinger, G.R.2    Lipkind, G.3    Drum, C.L.4    Hanck, D.A.5    Blumenthal, K.M.6
  • 25
    • 0027403280 scopus 로고
    • Primary structure and functional expression of a mouse inward rectifier potassium channel
    • Kubo, Y., T.J. Baldwin, Y.N. Jan, and L.Y. Jan. 1993. Primary structure and functional expression of a mouse inward rectifier potassium channel. Nature. 362:127-133.
    • (1993) Nature , vol.362 , pp. 127-133
    • Kubo, Y.1    Baldwin, T.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 27
    • 0027186445 scopus 로고
    • Isolation and pharmacological characterization of omega-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses
    • Lampe, R.A., P.A. Defeo, M.D. Davison, J. Young, J.L. Herman, R.C. Spreen, M.B. Horn, T.J. Mangano, and R.A. Keith. 1993. Isolation and pharmacological characterization of omega-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses. Mol. Pharmacol. 44:451-460.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 451-460
    • Lampe, R.A.1    Defeo, P.A.2    Davison, M.D.3    Young, J.4    Herman, J.L.5    Spreen, R.C.6    Horn, M.B.7    Mangano, T.J.8    Keith, R.A.9
  • 29
    • 0344256589 scopus 로고    scopus 로고
    • Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels
    • Lee, H.C., J.M. Wang, and K.J. Swartz. 2003. Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels. Neuron. 40:527-536.
    • (2003) Neuron , vol.40 , pp. 527-536
    • Lee, H.C.1    Wang, J.M.2    Swartz, K.J.3
  • 34
    • 0035023528 scopus 로고    scopus 로고
    • Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels
    • Li-Smerin, Y., and KJ. Swartz. 2001. Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels. J. Gen. Physiol. 117:205-218.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 205-218
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 35
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Lu, Z., A.M. Klem, and Y. Ramu. 2001. Ion conduction pore is conserved among potassium channels. Nature. 413:809-813.
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 36
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon, R. 1991. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature. 350:232-235.
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 37
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon, R., S.L. Cohen, A. Kuo, A. Lee, and B.T. Chait. 1998. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 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
  • 39
    • 0024426645 scopus 로고
    • Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor
    • MacKinnon, R., and C. Miller. 1989. Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor. Science. 245:1382-1385.
    • (1989) Science , vol.245 , pp. 1382-1385
    • MacKinnon, R.1    Miller, C.2
  • 40
    • 0033570060 scopus 로고    scopus 로고
    • Isolation, amino acid sequence and functional assays of SGTx1. The first toxin purified from the venom of the spider scodra griseipes
    • Marvin, L., E. De, P. Cosette, J. Gagnon, G. Molle, and C. Lange. 1999. Isolation, amino acid sequence and functional assays of SGTx1. The first toxin purified from the venom of the spider scodra griseipes. Eur. J. Biochem. 265:572-579.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 572-579
    • Marvin, L.1    De, E.2    Cosette, P.3    Gagnon, J.4    Molle, G.5    Lange, C.6
  • 41
    • 0031467725 scopus 로고    scopus 로고
    • Voltage-dependent inhibition of N- and P-type calcium channels by the peptide toxin omega-grammotoxin-SIA
    • McDonough, S.I., R.A. Lampe, R.A. Keith, and B.P. Bean. 1997a. Voltage-dependent inhibition of N- and P-type calcium channels by the peptide toxin omega-grammotoxin-SIA. Mol. Pharmacol. 52:1095-1104.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 1095-1104
    • McDonough, S.I.1    Lampe, R.A.2    Keith, R.A.3    Bean, B.P.4
  • 42
    • 0030978579 scopus 로고    scopus 로고
    • Alteration of P-type calcium channel gating by the spider toxin omega-Aga-IVA
    • McDonough, S.I., I.M. Mintz, and B.P. Bean. 1997b. Alteration of P-type calcium channel gating by the spider toxin omega-Aga-IVA. Biophys. J. 72:2117-2128.
    • (1997) Biophys. J. , vol.72 , pp. 2117-2128
    • McDonough, S.I.1    Mintz, I.M.2    Bean, B.P.3
  • 44
    • 0028983387 scopus 로고
    • + channel-blocking peptides
    • + channel-blocking peptides. Neuron. 15:5-10.
    • (1995) Neuron , vol.15 , pp. 5-10
    • Miller, C.1
  • 48
    • 0029645290 scopus 로고
    • Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A
    • Monks, S.A., P.K. Pallaghy, M.J. Scanlon, and R.S. Norton. 1995. Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A. Structure. 3:791-803.
    • (1995) Structure , vol.3 , pp. 791-803
    • Monks, S.A.1    Pallaghy, P.K.2    Scanlon, M.J.3    Norton, R.S.4
  • 52
    • 0026666693 scopus 로고
    • Mapping function to structure in a channel-blocking peptide: Electrostatic mutants of charybdotoxin
    • Park, C.S., and C. Miller. 1992b. Mapping function to structure in a channel-blocking peptide: electrostatic mutants of charybdotoxin. Biochemistry. 31:7749-7755.
    • (1992) Biochemistry , vol.31 , pp. 7749-7755
    • Park, C.S.1    Miller, C.2
  • 53
    • 0033742266 scopus 로고    scopus 로고
    • Peptides and genes coding for scorpion toxins that affect ion-channels
    • Possani, L.D., E. Merino, M. Corona, F. Bolivar, and B. Becerril. 2000. Peptides and genes coding for scorpion toxins that affect ion-channels. Biochimie. 82:861-868.
    • (2000) Biochimie , vol.82 , pp. 861-868
    • Possani, L.D.1    Merino, E.2    Corona, M.3    Bolivar, F.4    Becerril, B.5
  • 54
    • 0030064382 scopus 로고    scopus 로고
    • + channel selectivity filter by mutant cycle-based structure analysis
    • + channel selectivity filter by mutant cycle-based structure analysis. Neuron. 16:131-139.
    • (1996) Neuron , vol.16 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    MacKinnon, R.3
  • 55
    • 0034768977 scopus 로고    scopus 로고
    • Pharmacology and biochemistry of spider venoms
    • Rash, L.D., and W.C. Hodgson. 2002. Pharmacology and biochemistry of spider venoms. Toxicon. 40:225-254.
    • (2002) Toxicon , vol.40 , pp. 225-254
    • Rash, L.D.1    Hodgson, W.C.2
  • 60
    • 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. 33:443-450.
    • (1994) Biochemistry , vol.33 , pp. 443-450
    • Stampe, P.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 61
    • 0034103610 scopus 로고    scopus 로고
    • Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels
    • Suchyna, T.M., J.H. Johnson, K. Hamer, J.F. Leykam, D.A. Gage, H.F. Clemo, C.M. Baumgarten, and F. Sachs. 2000. Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels. J. Gen. Physiol. 115:583-598.
    • (2000) J. Gen. Physiol. , vol.115 , pp. 583-598
    • Suchyna, T.M.1    Johnson, J.H.2    Hamer, K.3    Leykam, J.F.4    Gage, D.A.5    Clemo, H.F.6    Baumgarten, C.M.7    Sachs, F.8
  • 62
    • 0038606006 scopus 로고    scopus 로고
    • Importance of the conserved aromatic residues in the scorpion α-like toxin BmK M1: The hydrophobic surface region revisited
    • Sun, Y.M., F. Bosmans, R.H. Zhu, C. Goudet, Y.M. Xiong, J. Tytgat, and D.C. Wang. 2003. Importance of the conserved aromatic residues in the scorpion α-like toxin BmK M1: the hydrophobic surface region revisited. J. Biol. Chem. 278:24125-24131.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24125-24131
    • Sun, Y.M.1    Bosmans, F.2    Zhu, R.H.3    Goudet, C.4    Xiong, Y.M.5    Tytgat, J.6    Wang, D.C.7
  • 63
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz, K.J., and R. MacKinnon. 1995. An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron. 15:941-949.
    • (1995) Neuron , vol.15 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 64
    • 0030952979 scopus 로고    scopus 로고
    • + channel through multiple binding sites
    • + channel through multiple binding sites. Neuron. 18:665-673.
    • (1997) Neuron , vol.18 , pp. 665-673
    • Swartz, K.J.1    MacKinnon, R.2
  • 67
    • 0036382850 scopus 로고    scopus 로고
    • Solution structure of w-grammotoxin SIA, a gating modifier of P/Q and N type calcium channels
    • Takeuchi, K., J.I. Kim, H. Takahashi, K. Swartz, and I. Shimada. 2002. Solution structure of w-grammotoxin SIA, a gating modifier of P/Q and N type calcium channels. J. Mol. Biol. 321:517-526.
    • (2002) J. Mol. Biol. , vol.321 , pp. 517-526
    • Takeuchi, K.1    Kim, J.I.2    Takahashi, H.3    Swartz, K.4    Shimada, I.5
  • 69
    • 0033767401 scopus 로고    scopus 로고
    • A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels
    • Winterfield, J.R., and K.J. Swartz. 2000. A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels. J. Gen. Physiol. 116:637-644.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 637-644
    • Winterfield, J.R.1    Swartz, K.J.2
  • 70
    • 0030951334 scopus 로고    scopus 로고
    • Identification of structural elements of a scorpion α-neurotoxin important for receptor site recognition
    • Zilberberg, N., O. Froy, E. Loret, S. Cestele, D. Arad, D. Gordon, and M. Gurevitz. 1997. Identification of structural elements of a scorpion α-neurotoxin important for receptor site recognition. J. Biol. Chem. 272:14810-14816.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14810-14816
    • Zilberberg, N.1    Froy, O.2    Loret, E.3    Cestele, S.4    Arad, D.5    Gordon, D.6    Gurevitz, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.