Solution structure of α-conotoxin MI determined by 1H-NMR spectroscopy and molecular dynamics simulation with the explicit solvent water

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1343, Issue 2, 1997, Pages 327-334

  Gouda, Hiroaki ^a   Yamazaki, Ken ichi ^b   Hasegawa, Jun ^b   Kobayashi, Yuji ^c   Nishiuchi, Yuji ^d   Sakakibara, Shumpei ^d   Hirono, Shuichi ^a  

^a KITASATO UNIVERSITY   (Japan)

^b DAIICHI SANKYO CO   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d Protein Research Foundation   (Japan)

Author keywords

2D NMR; Acetylcholine receptor; Conus magus; Molecular dynamics simulation; Neurotoxin; Solution structure

Indexed keywords

CONOTOXIN; NEUROTOXIN; NICOTINIC RECEPTOR; WATER;

ARTICLE; CONFORMATION; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; TOXIN STRUCTURE;

COMPUTER SIMULATION; CONOTOXINS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; MOLLUSK VENOMS; NICOTINIC ANTAGONISTS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES, CYCLIC; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, NICOTINIC; SEQUENCE HOMOLOGY, AMINO ACID; WATER;

CONUS MAGUS;

EID: 0031555380     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(97)00140-4     Document Type: Article

References (31)

1. Gray W.R., Luque A., Olivera B.M., Barrett J., Cruz L.J. Peptide toxins from Conus geographus venom. J. Biol. Chem. 256:1981;4734-4740.
2. McIntosh M., Cruz L.J., Hunkapiller M.W., Gray W.R., Olivera B.M. Isolation and structure of a peptide toxin from the marine snail Conus magus. Arch. Biochem. Biophys. 218:1982;329-334.
3. Cruz L.J., Gray W.R., Olivera B.M., Zeikus R.D., Kerr L., Yoshikami D., Moczydlowski E. Conus geographus toxins that discriminate between neuronal and muscle sodium channels. J. Biol. Chem. 260:1985;9280-9288.
4. Olivera B.M., McIntosh J.M., Cruz L.J., Luque F.A., Gray W.R. Purification and sequence of a presynaptic peptide toxin from Conus geographus venom. Biochemistry. 23:1984;5087-5090.
5. Gray W.R., Olivera B.M., Cruz L.J. Peptide toxins from venomous Conus snails. Annu. Rev. Biochem. 57:1988;665-700.
6. 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.
7. Utkin Y.N., Kobayashi Y., Hucho F., Tsetlin V.I. Relationship between the binding sites for an α-conotoxin and snake venom neurotoxins in the nicotinic acetylcholine receptor from Torpedo californica. Toxicon. 32:1994;1153-1157.
8. 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.
9. Hider R.C. A proposal for the structure of conotoxin - a potent antagonist of the nicotinic acetylcholine receptor. FEBS Lett. 184:1985;181-184.
10. W.R. Gray, D.M. Middlemas, R. Zeikus, B.M. Olivera, L.J. Cruz, Structure-activity relations in α-conotoxins: a model, in: C.M. Deber, V.J. Hruby, K.D. Kopple (Eds.), Peptides, Structure and Function, Pierce, Rockford, IL, 1985, pp. 823-832.
11. 1H nuclear magnetic resonance spectroscopy and distance geometry calculations Biochemistry. 28:1989;4853-4860.
12. Pardi A., Galdes A., Florance J., Maniconte D. Solution structures of α-conotoxin GI determined by two-dimensional NMR spectroscopy. Biochemistry. 28:1989;5494-5501.
13. Guddat L.W., Martin J.A., Shan L., Edmundson A.B., Gray W.R. Three-dimensional structure of the α-conotoxin GI at 1.2 Å resolution. Biochemistry. 35:1996;11329-11335.
14. Fox T., Kollman P.A. The application of different solvation and electrostatic models in molecular dynamics simulations of ubiquitin: how well is the X-ray structure "maintained"? Proteins. 25:1996;315-334.
15. Cheatham III T.E., Kollman P.A. Observation of the A-DNA to B-DNA transition during unrestrained molecular dynamics in aqueous solution. J. Mol. Biol. 259:1996;434-444.
16. Brunne R.M., Berndt K.D., Güntert P., Wüthrich K., van Gunsteren W.F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations. Proteins. 23:1995;49-62.
17. Smith L.J., Mark A.E., Dobson C.M., van Gunsteren W.F. Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes. Biochemistry. 34:1995;10918-10931.
18. Nishiuchi Y., Sakakibara S. Synthesis of conotoxin MI and GII: structure-activity relationship of conotoxins. Peptide Chemistry. 1983:1984;191-196.
19. 1H NMR spectra of proteins via double quantum filtering Biochem. Biophys. Res. Commun. 117:1983;479-485.
20. Bax A., Davis D.G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
21. Macura S., Huang Y., Suter D., Ernst R.R. Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. Magn. Reson. 43:1981;259-281.
22. Bax A., Davis D.G. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63:1985;207-213.
23. Mueller L. P.E.COSY, a simple alternative to E.COSY. J. Magn. Reson. 72:1987;191-196.
24. States D.J., Haberkorn R.A., Ruben D.J. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48:1982;286-292.
25. A.T. Brünger, X-PLOR Manual, Version 3.1, Yale University, New Haven, CT, USA, 1993.
26. D.A. Pearlman, D.A. Case, J.W. Caldwell, W.S. Ross, T.E. Cheatham III, D.M. Ferguson, G.L. Seibel, U.C. Singh, P.K. Weiner, P.A. Kollman, AMBER 4.1, University of California, San Francisco, 1995.
27. Cornell W.D., Cieplak P., Bayly C.I., Gould I.R., Merz Jr K.M., Ferguson D.M., Spellmeyer D.C., Fox T., Caldwell J.W., Kollman P.A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117:1995;5179-5197.
28. Gray W.R., Rivier J.E., Galyean R., Cruz L.J., Olivera B.M. Conotoxin MI. Disulfide bonding and conformational states. J. Biol. Chem. 258:1983;12247-12251.
29. Zafaralla G.C., Ramilo C., Gray W.R., Karlstrom R., Olivera B.M., Cruz L.J. Phylogenetic specificity of cholinergic ligands: α-conotoxin SI. Biochemistry. 27:1988;7102-7105.
30. Hashimoto K., Uchida S., Yoshida H., Nishiuchi Y., Sakakibara S., Yukari K. Structure-activity relations of conotoxins at the neuromuscular junction. Eur. J. Pharmacol. 118:1985;351-354.
31. Hann R.M., Pagán O.R., Eterović V.A. The α-conotoxins GI and MI distinguish between the nicotinic acetylcholine receptor agonist sites while SI does not. Biochemistry. 33:1994;14058-14063.