Toxins selective for subunit interfaces as probes of nicotinic acetylcholine receptor structure

Journal of Physiology Paris

Volumn 92, Issue 2, 1998, Pages 79-83

  Taylor, Palmer ^a   Osaka, Hitoshi ^a   Molles, Brian E ^a   Sugiyama, Naoya ^a,d   Marchot, Pascale ^a,e   Ackermann, Elizabeth J ^a   Malany, Siobhan ^a   McArdle, Joseph J ^b   Sine, Steven M ^c   Tsigelny, Igor ^a  

^a San Diego   (United States)

^b RUTGERS NEW JERSEY MEDICAL SCHOOL   (United States)

^c MAYO CLINIC   (United States)

^d YOKOHAMA CITY UNIVERSITY   (Japan)

^e CNRS   (France)

Author keywords

Homologous subunits; Ligand binding sites; Nicotinic acetylcholine receptor

Indexed keywords

ACETYLCHOLINE; ALPHA BUNGAROTOXIN; ALPHA TOXIN; CONOTOXIN; LOPHOTOXIN; NEUROTOXIN; NICOTINIC RECEPTOR; TUBOCURARINE CHLORIDE;

AMINO ACID SUBSTITUTION; BINDING AFFINITY; BINDING SITE; CHANNEL GATING; CHOLINERGIC SYSTEM; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; PROTEIN ASSEMBLY; PROTEIN PROTEIN INTERACTION; RECEPTOR AFFINITY; RECEPTOR BINDING; RECEPTOR INTRINSIC ACTIVITY; RECEPTOR SENSITIVITY; SEQUENCE HOMOLOGY;

EID: 0032458697     PISSN: 09284257     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0928-4257(98)80142-3     Document Type: Conference Paper

References (21)

1. [1] Ackermann E.J., Taylor P., Non-identity of the α-neurotoxin binding sites on the nicotinic acetylcholine receptor revealed by modification of neurotoxin and receptor structures, Biochemistry 36 (1997) 12836-12844.
2. [2] Ackermann E.J., Ang E.T.-M., Kanter J., Tsigelny I., Taylor P., Identification of pairwise interactions in the α-neurotoxin-nicotinic acetylcholine receptor complex, J. Biol. Chem. 273 (1998) 10958-10954.
3. [3] Bourne Y., Taylor P., Marchot P., Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex, Cell 83 (1995) 503-512.
4. [4] Changeux J.P., Chemical signaling in the brain, Sci. Am. 269 (1993) 58-62.
5. [5] Dennis M., Giraudat J., Kotzyba-Hibert F., Goeldner M., Hirth C., Chang J.-Y., Lazure C., Chretien M., Changeux J.-P., Amino acids of the Torpedo marmorata acetylcholine receptor α-subunit labeled by a photoaffinity ligand for the acetylcholine receptor binding site, Biochemistry 27 (1988) 2346-2357.
6. [6] Galzi J.L., Revah F., Black D., Goeldner M., Hirth C., Changeux J.-P., Identification of a novel amino acid α-Tyrosine 93 within the cholinergic ligand binding site of the acetylcholine receptor by photoaffinity labeling: Additional evidence for a three-loop model of the acetylcholine binding site, J. Biol. Chem. 265 (1990) 10430-10437.
7. [7] Harel M., Kleywegt G.J., Ravelli R.B.G., Silman I., Sussman J.L., Crystal structure of an acetylcholinesterase fasciculin complex: interaction of a three fingered toxin from snake venom with its target, Structure 3 (1995) 1355-1366.
8. [8] Karlin A., Akabas M., Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins, Neuron 15 (1995) 1231-1244.
9. [9] Kreienkamp H.J., Maeda R.K., Sine S.M., Taylor P., Intersubunit contacts governing assembly of the mammalian nicotinic acetylcholine receptor, Neuron 14 (1995) 635-644.
10. [10] Kreienkamp H.-J., Sine S.M., Maeda R.K., Taylor P., Glycosylation sites selectively interfere with α-toxin binding to the nicotinic acetylcholine receptor, J. Biol. Chem. 269 (1994) 8108-8114.
11. [11] Lee C.Y., Isolation of neurotoxins from the venom of Bungarus multicintus and their modes of neuromuscular blocking action, Arch. Int. Pharmacodyn. Ther. 144 (1963) 241-257.
12. [12] O'Leary M.E., White M.M., Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor, J. Biol. Chem. 267 (1992) 8360-8365.
13. [13] Oswald R.E., Changeux J.P., Cross-linking of α-bungarotoxin to the acetylcholine receptor from Torpedo marmorata by ultra violet-light irradiation, FEBS Lett. 139 (1982) 225-229.
14. [14] Sine S.M., Quiram P., Papanikolaou F., Kreienkamp H.-J., Taylor P., Conserved tyrosines in the α subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists, J. Biol. Chem. 269 (1994) 8808-8816.
15. [15] Sine S.M., Kreienkamp H.-J., Bren N., Maeda R., Taylor P., Molecular dissection of subunit interfaces in the acetylcholine receptor. Identification of determinants of α-conotoxin M1 selectivity, Neuron 15 (1995) 205-211.
16. [16] Sugiyama N., Boyd A.E., Taylor P., Anionic residues in the α-subunit of the nicotinic acetylcholine receptor contributing to subunit assembly and ligand binding, J. Biol. Chem. 271 (1996) 26575-26581.
17. [17] Sugiyama N., Marchot P., Kawanishi C., Osaka H., Molles B., Sine S.M., Taylor, P., Residues at the subunit interfaces of the nicotinic acetylcholine receptor that contribute to α-conotoxin M1 binding, Mol. Pharmacol. 52 (1998) 787-794.
18. [18] Tomaselli G.F., McLaughlin J.T., Jurman M.E., Hawrot E., Yellen G., Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor, Biophys. J. 60 (1991) 721-727.
19. [19] Tremeau O., Lemaire C., Drevet P., Pikasfeld S., Ducancel F., Boulain J-C., Meńez A., Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, J. Biol. Chem. 270 (1995) 9362-9369.
20. [20] Tsai M.C., Hsieh W.H., Smith L.A., Lee C.Y., Effects of waglerin 1 on neuromuscular transmission of mouse nerve-muscle preparations, Toxicon 33 (1995) 363-371.
21. [21] Tsigelny I., Sugiyama N., Sine S.M., Taylor P., A model of the nicotinic receptor extracellular domain based on sequence identity and residue location, Biophys. J. 73 (1997) 52-66.