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Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin.

Chagot B, Diochot S, Pimentel C, Lazdunski M, Darbon H
Proteins 59 380-6 (2005)
Cited: 27 times
EuropePMC logo PMID: 15726634

Abstract

APETx1 is a 42-amino acid toxin purified from the venom of the sea anemone Anthopleura elegantissima. This cysteine-rich peptide possesses three disulfide bridges (C4-C37, C6-C30, and C20-C38). Its pharmacological target is the Ether-a-gogo potassium channel. We herein determine the solution structure of APETx1 by use of conventional two-dimensional 1H-NMR techniques followed by torsion angle dynamics and refinement protocols. The calculated structure of APETx1 belongs to the disulfide-rich all-beta structural family, in which a three-stranded anti-parallel beta-sheet is the only secondary structure. APETx1 is the first Ether-a-gogo effector discovered to fold in this way. We therefore compare the structure of APETx1 to those of the two other known effectors of the Ether-a-gogo potassium channel, CnErg1 and BeKm-1, and analyze the topological disposition of key functional residues proposed by analysis of the electrostatic anisotropy. The interacting surface is made of a patch of aromatic residues (Y5, Y32, and F33) together with two basic residues (K8 and K18) at the periphery of the surface. We pinpoint the absence of the central lysine present in the functional surface of the two other Ether-a-gogo effectors.

Reviews - 1wqk mentioned but not cited (2)

  1. Sea anemone (Cnidaria, Anthozoa, Actiniaria) toxins: an overview. Frazão B, Vasconcelos V, Antunes A. Mar Drugs 10 1812-1851 (2012)
  2. Marine Toxins Targeting Kv1 Channels: Pharmacological Tools and Therapeutic Scaffolds. Finol-Urdaneta RK, Belovanovic A, Micic-Vicovac M, Kinsella GK, McArthur JR, Al-Sabi A. Mar Drugs 18 E173 (2020)

Articles - 1wqk mentioned but not cited (5)

  1. Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels. Chagot B, Escoubas P, Diochot S, Bernard C, Lazdunski M, Darbon H. Protein Sci 14 2003-2010 (2005)
  2. Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins. Chen Z, Luo F, Feng J, Yang W, Zeng D, Zhao R, Cao Z, Liu M, Li W, Jiang L, Wu Y. PLoS One 8 e60201 (2013)
  3. APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel KV10.1. Moreels L, Peigneur S, Galan DT, De Pauw E, Béress L, Waelkens E, Pardo LA, Quinton L, Tytgat J. Mar Drugs 15 (2017)
  4. APETx-Like Peptides from the Sea Anemone Heteractis crispa, Diverse in Their Effect on ASIC1a and ASIC3 Ion Channels. Kalina RS, Koshelev SG, Zelepuga EA, Kim NY, Kozlov SA, Kozlovskaya EP, Monastyrnaya MM, Gladkikh IN. Toxins (Basel) 12 (2020)
  5. Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization. Matsumura K, Shimomura T, Kubo Y, Oka T, Kobayashi N, Imai S, Yanase N, Akimoto M, Fukuda M, Yokogawa M, Ikeda K, Kurita JI, Nishimura Y, Shimada I, Osawa M. BMC Mol Cell Biol 22 3 (2021)


Reviews citing this publication (10)

  1. hERG K(+) channels: structure, function, and clinical significance. Vandenberg JI, Perry MD, Perrin MJ, Mann SA, Ke Y, Hill AP. Physiol Rev 92 1393-1478 (2012)
  2. Structures of sea anemone toxins. Norton RS. Toxicon 54 1075-1088 (2009)
  3. Novel peptide toxins recently isolated from sea anemones. Shiomi K. Toxicon 54 1112-1118 (2009)
  4. Toxins interacting with ether-à-go-go-related gene voltage-dependent potassium channels. Wanke E, Restano-Cassulini R. Toxicon 49 239-248 (2007)
  5. Venom-derived peptide inhibitors of voltage-gated potassium channels. Norton RS, Chandy KG. Neuropharmacology 127 124-138 (2017)
  6. Toxin modulators and blockers of hERG K(+) channels. Jiménez-Vargas JM, Restano-Cassulini R, Possani LD. Toxicon 60 492-501 (2012)
  7. Sea Anemone Toxins: A Structural Overview. Madio B, King GF, Undheim EAB. Mar Drugs 17 (2019)
  8. Mechanisms of Action of the Peptide Toxins Targeting Human and Rodent Acid-Sensing Ion Channels and Relevance to Their In Vivo Analgesic Effects. Verkest C, Salinas M, Diochot S, Deval E, Lingueglia E, Baron A. Toxins (Basel) 14 709 (2022)
  9. Peptide Toxins Targeting KV Channels. Matsumura K, Yokogawa M, Osawa M. Handb Exp Pharmacol 267 481-505 (2021)
  10. The Anemonia viridis Venom: Coupling Biochemical Purification and RNA-Seq for Translational Research. Nicosia A, Mikov A, Cammarata M, Colombo P, Andreev Y, Kozlov S, Cuttitta A. Mar Drugs 16 (2018)

Articles citing this publication (10)

  1. A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. Peigneur S, Béress L, Möller C, Marí F, Forssmann WG, Tytgat J. FASEB J 26 5141-5151 (2012)
  2. APETx1 from sea anemone Anthopleura elegantissima is a gating modifier peptide toxin of the human ether-a-go-go- related potassium channel. Zhang M, Liu XS, Diochot S, Lazdunski M, Tseng GN. Mol Pharmacol 72 259-268 (2007)
  3. Species diversity and peptide toxins blocking selectivity of ether-a-go-go-related gene subfamily K+ channels in the central nervous system. Restano-Cassulini R, Korolkova YV, Diochot S, Gurrola G, Guasti L, Guasti L, Possani LD, Lazdunski M, Grishin EV, Arcangeli A, Wanke E. Mol Pharmacol 69 1673-1683 (2006)
  4. Crotamine pharmacology revisited: novel insights based on the inhibition of KV channels. Peigneur S, Orts DJ, Prieto da Silva AR, Oguiura N, Boni-Mitake M, de Oliveira EB, Zaharenko AJ, de Freitas JC, Tytgat J. Mol Pharmacol 82 90-96 (2012)
  5. Revisiting venom of the sea anemone Stichodactyla haddoni: Omics techniques reveal the complete toxin arsenal of a well-studied sea anemone genus. Madio B, Undheim EAB, King GF. J Proteomics 166 83-92 (2017)
  6. Peptide fingerprinting of the neurotoxic fractions isolated from the secretions of sea anemones Stichodactyla helianthus and Bunodosoma granulifera. New members of the APETx-like family identified by a 454 pyrosequencing approach. Rodríguez AA, Cassoli JS, Sa F, Dong ZQ, de Freitas JC, Pimenta AM, de Lima ME, Konno K, Lee SM, Garateix A, Zaharenko AJ. Peptides 34 26-38 (2012)
  7. The enigma of the near-symmetry of proteins: Domain swapping. Bonjack-Shterengartz M, Avnir D. PLoS One 12 e0180030 (2017)
  8. The near-symmetry of proteins. Bonjack-Shterengartz M, Avnir D. Proteins 83 722-734 (2015)
  9. Defensin-neurotoxin dyad in a basally branching metazoan sea anemone. Kim CH, Lee YJ, Go HJ, Oh HY, Lee TK, Park JB, Park NG. FEBS J 284 3320-3338 (2017)
  10. PhcrTx2, a New Crab-Paralyzing Peptide Toxin from the Sea Anemone Phymanthus crucifer. Rodríguez AA, Garateix A, Salceda E, Peigneur S, Zaharenko AJ, Pons T, Santos Y, Arreguín R, Ständker L, Forssmann WG, Tytgat J, Vega R, Soto E. Toxins (Basel) 10 (2018)


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