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NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.

Zeng H, Hawrot E
J Biol Chem 277 37439-45 (2002)
Cited: 20 times
EuropePMC logo PMID: 12133834

Abstract

The alpha18-mer peptide, spanning residues 181-198 of the Torpedo nicotinic acetylcholine receptor alpha1 subunit, contains key binding determinants for agonists and competitive antagonists. To investigate whether the alpha18-mer can bind other alpha-neurotoxins besides alpha-bungarotoxin, we designed a two-dimensional (1)H-(15)N heteronuclear single quantum correlation experiment to screen four related neurotoxins for their binding ability to the peptide. Of the four toxins tested (erabutoxin a, erabutoxin b, LSIII, and alpha-cobratoxin), only alpha-cobratoxin binds the alpha18-mer to form a 1:1 complex. The NMR solution structure of the alpha-cobratoxin.alpha18-mer complex was determined with a backbone root mean square deviation of 1.46 A. In the structure, alpha-cobratoxin contacts the alpha18-mer at the tips of loop I and II and through C-terminal cationic residues. The contact zone derived from the intermolecular nuclear Overhauser effects is in agreement with recent biochemical data. Furthermore, the structural models support the involvement of cation-pi interactions in stabilizing the complex. In addition, the binding screen results suggest that C-terminal cationic residues of alpha-bungarotoxin and alpha-cobratoxin contribute significantly to binding of the alpha18-mer. Finally, we present a structural model for nicotinic acetylcholine receptor-alpha-cobratoxin interaction by superimposing the alpha-cobratoxin.alpha18-mer complex onto the crystal structure of the acetylcholine-binding protein (Protein Data Bank code ).

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Reviews citing this publication (5)

  1. Snake and snail toxins acting on nicotinic acetylcholine receptors: fundamental aspects and medical applications. Tsetlin VI, Hucho F. FEBS Lett 557 9-13 (2004)
  2. Nicotinic acetylcholine receptor inhibitors derived from snake and snail venoms. Dutertre S, Nicke A, Tsetlin VI. Neuropharmacology 127 196-223 (2017)
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  1. Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors. Bourne Y, Talley TT, Hansen SB, Taylor P, Marchot P. EMBO J 24 1512-1522 (2005)
  2. Toxin insights into nicotinic acetylcholine receptors. Dutertre S, Lewis RJ. Biochem Pharmacol 72 661-670 (2006)
  3. Inhibition of Naja kaouthia venom activities by plant polyphenols. Pithayanukul P, Ruenraroengsak P, Bavovada R, Pakmanee N, Suttisri R, Saen-oon S. J Ethnopharmacol 97 527-533 (2005)
  4. Competition of drugs to serum albumin in combination therapy. Sułkowska A, Bojko B, Równicka J, Sułkowski W. Biopolymers 74 256-262 (2004)
  5. Vicinal disulfide bridge conformers by experimental methods and by ab initio and DFT molecular computations. Hudáky I, Gáspári Z, Carugo O, Cemazar M, Pongor S, Perczel A. Proteins 55 152-168 (2004)
  6. Towards structure determination of neurotoxin II bound to nicotinic acetylcholine receptor: a solid-state NMR approach. Krabben L, van Rossum BJ, Castellani F, Bocharov E, Schulga AA, Arseniev AS, Weise C, Hucho F, Oschkinat H. FEBS Lett 564 319-324 (2004)
  7. Induced folding in RNA recognition by Arabidopsis thaliana DCL1. Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. Nucleic Acids Res 43 6607-6619 (2015)
  8. Drysdalin, an antagonist of nicotinic acetylcholine receptors highlights the importance of functional rather than structural conservation of amino acid residues. Chandna R, Tae HS, Seymour VAL, Chathrath S, Adams DJ, Kini RM. FASEB Bioadv 1 115-131 (2019)
  9. C-terminus of a long alpha-neurotoxin is highly mobile when bound to the nicotinic acetylcholine receptor: a time-resolved fluorescence anisotropy approach. Johnson DA. Biophys Chem 116 213-218 (2005)
  10. Rediocides A and G as potential antitoxins against cobra venom. Utsintong M, Kaewnoi A, Leelamanit W, Olson AJ, Vajragupta O. Chem Biodivers 6 1404-1414 (2009)
  11. Animal Venom Peptides Cause Antinociceptive Effects by Voltage-gated Calcium Channels Activity Blockage. Trevisan G, Oliveira SM. Curr Neuropharmacol 20 1579-1599 (2022)
  12. Spatial Structure and Activity of Synthetic Fragments of Lynx1 and of Nicotinic Receptor Loop C Models. Mineev KS, Kryukova EV, Kasheverov IE, Egorova NS, Zhmak MN, Ivanov IA, Senko DA, Feofanov AV, Ignatova AA, Arseniev AS, Utkin YN, Tsetlin VI. Biomolecules 11 (2020)


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