An improved solution structure for ψ-conotoxin PIIIE

Biochemistry

Volumn 42, Issue 21, 2003, Pages 6347-6352

  Van Wagoner, Ryan M ^a,b   Ireland, Chris M ^a  

^a UNIVERSITY OF UTAH   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANNEALING; CONFORMATIONS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

MOLECULAR MODELING;

BIOCHEMISTRY;

CARBON 13; CONOTOXIN; CYSTEINE; DISULFIDE; NICOTINIC RECEPTOR; NICOTINIC RECEPTOR BLOCKING AGENT; PEPTIDE; PROTON; PSI CONOTOXIN PIIIE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CALCULATION; COVALENT BOND; DISULFIDE BOND; ELECTRIC POTENTIAL; GEOMETRY; ISOTOPE LABELING; MOLECULAR MODEL; MUTATIONAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; SIMULATION; STRUCTURE ANALYSIS; TECHNIQUE; TOXIN ANALYSIS; TOXIN STRUCTURE;

ALGORITHMS; CYSTEINE; DISULFIDES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MODELS, THEORETICAL; MUTATION; OMEGA-CONOTOXINS; PEPTIDE BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STEREOISOMERISM;

INVERTEBRATA;

EID: 0038348783     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027274e     Document Type: Article

References (39)

1. Mitchell, S. S., Shon, K. J., Foster, M. P., Davis, D. R., Olivera, B. M., and Ireland, C. M. (1998) Biochemistry 37, 1215-1220.
2. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., and Bourne, P. E. (2000) Nucleic Acids Res. 28, 235-242.
3. Van Wagoner, R. M. (2001) PhD Dissertation, Department of Medicinal Chemistry, University of Utah, Salt Lake City.
4. Atkinson, R. A., Kieffer, B., Dejaegere, A., Sirockin, F., and Lefevre, J. F. (2000) Biochemistry 39, 3908-3919.
5. Rigby, A. C., Lucas-Meunier, E., Kalume, D. E., Czerwiec, E., Hambe, B., Dahlqvist, I., Fossier, P., Baux, G., Roepstorff, P., Baleja, J. D., Furie, B. C., Furie, B., and Stenflo, J. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 5758-5763.
6. Maslennikov, I. V., Sobol, A. G., Gladky, K. V., Lugovskoy, A. A., Ostrovsky, A. G., Tsetlin, V. I., Ivanov, V. T., and Arseniev, A. S. (1998) Eur. J. Biochem. 254, 238-247.
7. Bodanszky, M., and Bodanszky, A. (1994) in The Practice of Peptide Synthesis, pp 68-69, Springer-Verlag, New York.
8. Atherton, E., and Sheppard, R. C. (1989) in Solid-Phase Peptide Synthesis, p 60, IRL Press, New York.
9. Fields, G. B., and Noble, R. L. (1990) Int. J. Peptide Protein Res. 35, 161-214.
10. Hopkins, C., Grilley, M., Miller, C., Shon, K. J., Cruz, L. J., Gray, W. R., Dykert, J., Rivier, J., Yoshikami, D., and Olivera, B. M. (1995) J. Biol. Chem. 270, 22361-22367.
11. Shon, K. J., Grilley, M., Jacobsen, R. B., Cartier, G. E., Hopkins, C., Gray, W. R., Watkins, M., Hillyard, D. R., Rivier, J., Torres, J., Yoshikami, D., and Olivera, B. M. (1997) Biochemistry 36, 9581-9587.
12. Braunschweiler, L., and Ernst, R. R. (1983) J. Magn. Reson. 53, 521-528.
13. Rance, M., Sørensen, O. W., Bodenhausen, G., Wagner, G., Ernst, R. R., and Wüthrich, K. (1983) Biochem. Biophys. Res. Commun. 117, 479-485.
14. Palmer, A. G., III, Cavanagh, J., Byrd, R. A., and Rance, M. (1992) J. Magn. Reson. 96, 416-424.
15. Mori, S., Abeygunawardana, C., Johnson, M. O., and van Zijl, P. C. (1995) J. Magn. Reson. B 108, 94-98.
16. Jeener, J., Meier, B. H., Bachmann, P., and Ernst, R. R. (1979) J. Chem. Phys. 71, 4546-4553.
17. Mueller, L. (1987) J. Magn. Reson. 72, 191-196.
18. Folkers, P. J. M., Folmer, R. H. A., Konings, R. N. H., and Hilbers, C. W. (1993) J. Am. Chem. Soc. 115, 3798-3799.
19. Hu, H., and Shaka, A. J. (1999) J. Magn. Reson. 136, 54-62.
20. Smallcombe, S. H., Patt, S. L., and Kiefer, P. A. (1995) J. Magn. Reson. A 117, 295-303.
21. Piotto, M., Saudek, V., and Sklenar, V. (1992) J. Biomol. NMR 2, 661-665.
22. States, D. J., Haberkorn, R. A., and Ruben, D. J. (1982) J. Magn. Reson. 48, 286-292.
23. Geen, H., and Freeman, R. (1991) J. Magn. Reson. 93, 93-141.
24. Guntert, P., and Wiithrich, K. (1992) J. Magn. Reson. 96, 403-407.
25. Boelens, R., Koning, T. M. G., and Kaptein, R. (1988) J. Mol. Struct. 173, 299-311.
26. Boelens, R., Koning, T. M. G., van der Marel, G. A., van Boom, J. H., and Kaptein, R. (1989) J. Magn. Reson. 82, 290-308.
27. DeMarco, A., Llinás, M., and Wüthrich, K. (1978) Biopolymers 17, 617-636.
28. Hyberts, S. G., Marki, W., and Wagner, G. (1987) Eur. J. Biochem. 164, 625-635.
29. Nilges, M., Clore, G. M., and Gronenborn, A. M. (1988) FEBS Lett. 229, 317-324.
30. Dauber-Osguthorpe, P., Roberts, V. A., Osguthorpe, D. J., Wolff, J., Genest, M., and Hagler, A. T. (1988) Proteins 4, 31-47.
31. Koradi, R., Billeter, M., and Wüthrich, K. (1996) J. Mol. Graphics 14, 51-55.
32. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley-Interscience, New York.
33. Pardi, A., Billeter, M., and Wüthrich, K. (1984) J. Mol. Biol. 180, 741-751.
34. Thomas, P. D., Basus, V. J., and James, T. L. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 1237-1241.
35. Crippen, G. M., and Havel, T. M. (1988) Distance Geometry and Molecular Conformation, Research Studies Press, Taunton, England.
36. Ramachandran, G. N., and Sasisekharan, V. (1968) Adv. Protein Chem. 23, 283-438.
37. Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) J. Biomol. NMR 8, 477-486.
38. Martí-Renom, M. A., Stote, R. H., Querol, E., Aviles, F. X., and Karplus, M. (2000) Proteins: Struct., Funct., Genet. 40, 482-493.
39. Craik, D. J., Daly, N. L., and Waine, C. (2001) Toxicon 39, 43-60.