Two distinct structures of α-conotoxin GI in aqueous solution

European Journal of Biochemistry

Volumn 254, Issue 2, 1998, Pages 238-247

  Maslennikov, Innokenty V ^a   Sobol, Alexander G ^a   Gladky, Konstantin V ^a   Lugovskoy, Alexey A ^a   Ostrovsky, Andrey G ^a   Tsetlin, Victor I ^a   Ivanov, Vadim T ^a   Arseniev, Alexander S ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Conformational analysis; Conotoxin; Nicotinic acetylcholine receptor; NMR

Indexed keywords

CONOTOXIN;

AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; TOXIN ANALYSIS; TOXIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; CONOTOXINS; CRYSTALLOGRAPHY, X-RAY; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLLUSK VENOMS; PEPTIDES, CYCLIC; PROTEIN CONFORMATION; SOLUTIONS; WATER;

EID: 0032102261     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2540238.x     Document Type: Article

References (34)

1. Myers, R. A., Cruz, L. J., Rivier, J. E. & Olivera, B. M. (1993) Conus peptides as chemical probes for receptors and ion channels, Chem. Rev. 93, 1923-1936.
2. Fainzilber, M., Hasson, A., Oren, R., Burlingame, A. L., Gordon, D., Spira, M. E. & Zlotkin, E. (1994) New mollusk-specific α-conotoxins block Aplysia neuronal acetylcholine receptors, Biochemistry 33, 9523-9529.
3. Utkin, Yu. N., Kobayashi, Y., Hucho, F. & Tsetlin, V. I. (1994) Relationship between the binding sites for an α-conotoxin and snake venom neurotoxins in the nicotinic acetylcholine receptor from Torpedo californica, Toxicon 32, 1153-1157.
4. Hann, R. M., Pagan, O. R. & Eterovic, V. A. (1994) The α-conotoxins GI and MI distinguish between the nicotinic acetylcholine receptor agonist sites while SI does not, Biochemistry 33, 14058-14063.
5. Groebe, D. R., Dumm, J. M., Levitan, E. S. & Abramson, S. N. (1995) α-Conotoxins selectively inhibit one of the two acetylcholine binding sites of nicotinic receptors, Mol. Pharmacol. 48, 105-111.
6. Groebe, D. R., Gray, W. R. & Abramson, S. N. (1997) Determinants involved in the affinity of α-conotoxins GI and SI for the muscle subtype of nicotinic acetylcholine receptors. Biochemistry 36, 6469-6474.
7. Hann, R. M., Pagan, O. R., Gregory, L. M., Jacome, T. & Eterovic, V. A. (1997) The 9-arginine residue of a-conotoxin GI is responsible for its selective high affinity for the ay agonist site on the electric organ acetylcholine receptor, Biochemistry 36, 9051-9056.
8. Guddat, L. W., Martin, J. A., Shan, L., Edmundson, A. B. & Gray, W. R. (1996) Three-dimensional structure of the α-conotoxin GI at 1.2 Å resolution, Biochemistry 35, 11 329-11 335.
9. Pardi, A., Galdes, A., Florance, J. & Maniconte, D. (1989) Solution structures of α-conotoxin GI determined by two-dimensional NMR spectroscopy, Biochemistry 28, 5494-5501.
10. 1H nuclear magnetic resonance spectroscopy and distance geometry calculations. Biochemistry 28, 4853-4860.
11. Kessler, H., Griesinger, C., Lautz, J., Muller, A., van Gunsteren, W. F. & Berendsen, H. J. C. (1988) Conformational dynamics detected by nuclear magnetic resonance NOE values and J coupling constants, J. Am. Chem. Soc. 110, 3393-3396.
12. Torda, A. E., Scheek, R. M. & van Gunsteren, W. F. (1990) Time-averaged nuclear Overhauser effect distance restraints applied to tendamistat, J. Mol. Biol. 214, 223-235.
13. Perlman, D. A. & Kollman, P. A. (1991) Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA, J. Mol. Biol. 220, 457-479.
14. Torda, A. E., Brunne, R. M., Huber, T., Kessler, H. & van Gunsteren, W. F. (1993) Structure refinement using time-averaged J-coupling constant restraints, J. Biomol. NMR 3, 55-66.
15. Bonvin, A. M. J. J., Boelens, R. & Kaptein, R. (1994) Time-and ensemble-averaged direct NOE restraints, J. Biomol. NMR 4, 143-149.
16. Vesterman, B., Saulitis, J., Betins, J., Liepins, E. & Nikiforovich, G. V. (1989) Dynamic space structure of the Leu-enkephalin molecule in DMSO solution, Biochim. Biophys. Acta 998, 204-209.
17. Mierke, D. F., Kurz, M. & Kassler, H. (1994) Peptide flexibility and calculations of an ensemble of molecules, J. Am. Chem. Soc. 116, 1042-1049.
18. Kemmink, J. & Scheek, R. M. (1995) Dynamics modelling of a helical peptide in solution using NMR data: Multiple conformations and multi-spin effects, J. Biomol. NMR 5, 33-40.
19. 1H-NMR spectra of protein via double quantum filter, Biochem. Biophys. Res. Commun. 117, 479-485.
20. Bax, A. & Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, J. Magn. Reson. 65, 355-366.
21. Jeener, J., Meir, G. N., Bachman, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553.
22. States, D. J., Habercorn, R. A. & Ruben, D. J. (1982) 2D NOE with pure absorption phase in four quadrants, J. Magn. Reson. 48, 286-292.
23. Bartels, C., Xia, T.-H., Billeter, M., Guntert, P. & Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR 6, 1-10.
24. Guntert, P., Braun, W. & Wüthrich, K. (1991) Efficient computation of 3D protein structures in solution from NMR data using the program DIANA and supporting programs CALIBA, HABAS and GLOMSA, J. Mol. Biol. 217, 517-530.
25. Borgias, B. A. & James, T. L. (1990) MARDIGRAS - a procedure for matrix analysis of relaxation for peptide geometry of an aqueous structure, J. Magn. Reson. 87, 475-487.
26. Kelley, L. A., Gardner, S. P. & Sutcliffe, M. J. (1996) An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally related subfamilies, Protein Eng. 9, 1063-1065.
27. Keepers, J. W. & James, T. L. (1984) A theoretical study of distance determinations from NMR. Two dimensional nuclear Overhauser effects spectra, J. Magn. Reson. 57, 404-426.
28. Haskell, K. H. & Hanson, R. J. (1981) An algorithm for linear least squares problems with equality and nonnegativity constraints, Math. Program. 21, 98-118.
29. Bystrov, V. F. (1976) Spin-spin coupling and conformational states of peptide systems, Progr. Nucl. Magn. Reson. Spectrosc. 10, 41-81.
30. Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.
31. Wüthrich, K. (1986) NMR of proteins and nucleic acids. John Wiley & Sons, New York.
32. Koning, T. M. G., Boelens, R. & Kaptein, R. (1990) Calculation of the nuclear Overhauser effect and the determination of proton-proton distances in the presence of internal motions, J. Magn. Reson. 90, 111-123.
33. Han, K. H., Hwang, K. J., Kim, S. M., Kim, S. K., Gray, W. R., Olivera, B. M., Rivier, J. & Shon, K. J. (1997) NMR structure determination of a novel conotoxin, [Pro 7,13] αA-conotoxin PIVA, Biochemistry 36, 1669-1677.
34. Olivera, B. M., Hiiyard, D. R., Marsh, M. & Yoshikami, D. (1995) Combinatorial peptide libraries in drug design: lessons from venomous cone snails, Trends Biotechnol. 13, 422-426.