Solution NMR analysis of the binding mechanism of DIVS6 model peptides of voltage-gated sodium channels and the lipid soluble alkaloid veratridine

Bioorganic and Medicinal Chemistry

Volumn 20, Issue 9, 2012, Pages 2796-2802

  Yoshinaka Niitsu, Ai ^a   Yamagaki, Tohru ^a,b   Harada, Masanori ^a   Tachibana, Kazuo ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b SUNTORY INSTITUTE FOR BIOORGANIC RESEARCH   (Japan)

Author keywords

Interaction mechanism; Model peptides; Neurotoxic alkaloid; NMR; Sodium channel

Indexed keywords

LYSYLLYSYLLYSYLSERYLTYROSYLISOLEUCYLISOLEUCYLISOLEUCYLSERYLPHENYLALANYLLEUCYLISOLEUCYLVALYLVALYLASPARAGINYLMETHIONYLTYROSYLISOLEUCYLALANYLISOLEUCYLISOLEUCYLLEUCYLGLUTAMYLLYSYLLYSYLLYSINE AMIDE; SERYLLYSYLISOLEUCYLISOLEUCYLLYSYLSERYLPHENYLALANYLLEUCYLLYSYLVALYLVALYLASPARAGINYLLYSYLTYROSYLISOLEUCYLALANYLISOLEUCYLISOLEUCYLLEUCYLGLUTAMIC ACID AMIDE; SODIUM CHANNEL NAV1.4; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; VERATRIDINE;

ALPHA HELIX; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; DRUG DESIGN; DRUG EFFICACY; DRUG PROTEIN BINDING; DRUG STRUCTURE; DRUG SYNTHESIS; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; POINT MUTATION; RAT; STRUCTURE ANALYSIS; TOXIN ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS; SODIUM CHANNELS; VERATRIDINE;

LILIUM; RATTUS;

EID: 84859894614     PISSN: 09680896     EISSN: 14643391     Source Type: Journal    
DOI: 10.1016/j.bmc.2012.03.034     Document Type: Article

References (32)

1. W.A. Catterall Neuron 26 2000 13
2. F.H. Yu, and W.A. Catterall Genome Biol. 4 2003 207
3. A.J. Wada Pharmacol. Sci. 102 2006 253
4. V. Yarov-Yarovoy, W.A. Catterall, S. Ceste, F.H. Yu, K. Konoki, and T. Scheuer Toxicon 49 2007 124
5. N.W. Plummer, and M.H. Meisler Genomics 57 1999 323
6. C.A. Hubner, and T.J. Jentsch Hum. Mol. Genet. 11 2002 2435
7. W.A. Catterall, S. Dib-Hajj, M.H. Meisler, and D. Pietrobon J. Neurol.Sci. 28 2008 11768
8. H.R. Guy, and P. Seetharamulu Proc. Natl. Acad. Sci. U.S.A. 83 1986 508
9. S.Y. Wang, and G.K. Wang Proc. Natl. Acad. Sci. U.S.A. 95 1998 2653
10. S. Pelletier, and W.A. Jacobs J. Am. Chem. Soc. 75 1953 3248
11. X. Zang, E.K. Fukuda, and J.D. Rosen J. Agric. Food Chem. 45 1997 1758
12. I. Ujvary, B.K. Eya, R.L. Grendell, R.F. Toia, and J.E. Casida J. Agric. Food Chem. 1991 1875 39
13. A. Niitsu, M. Harada, T. Yamagaki, and K. Tachibana Bioorg. Med. Chem. 16 2008 3025
14. V.L. Trainer, G.B. Brown, and W.A. Catterall J. Biol. Chem. 271 1996 11261
15. G.K. Wang, C. Quan, M. Seaver, and S.Y. Wang Pflugers Arch. 439 2000 705
16. S. Wang, and G.K. Wang Cell. Signal. 15 2003 151
17. T. Anger, D.J. Madge, M. Mulla, and D. Riddall J. Med. Chem. 44 2001 115
18. H.R. Arias Mar. Drugs 4 2006 37
19. J. Payandeh, T. Scheuer, N. Zheng, and W.A. Catterall Nature 475 2011 353
20. E. Schnur, M. Turkov, R. Kahn, D. Gordon, M. Gurevitz, and J. Anglister Biochemistry 47 2008 911
21. L. Otvos Jr, G.I. Szendrei, V.M. Lee, and H.H. Mantsch Eur. J. Biochem. 211 1993 249
22. K.R. Wang, B.Z. Zhang, W. Zhang, J.X. Yan, J. Li, and R. Wang Peptides 29 2008 963
23. S.L. Fornili, R. Pizzi, and D. Rebeccani Int. J. Pept. Res. Ther. 16 2010 223
24. C. Schwieters, J. Kuszewski, N. Tjandra, and G. Clore J. Magn. Res. 160 2003 65
25. C. Schwieters, J. Kuszewski, and G. Clore Prog. Nucl. Magn. Reson. Spectrosc. 48 2006 47
26. W. Humphrey J. Mol. Graphics Modell. 14 1996 33
27. R. Woody, and I. Tinoco J. Chem. Phys. 46 1967 4927
28. K. Wuthrich Biopolymers 22 1983 131
29. M. Sarker, A.J. Waring, F.J. Walther, K.M.W. Keough, and V. Booth Biochemistry 46 2007 11047
30. N.J. Linford, A.R. Cantrell, Y. Qu, T. Scheuer, and W.A. Catterall Proc. Natl. Acad. Sci. U.S.A. 95 1998 13947
31. S.Y. Wang, and G.K. Wang Biophys. J. 76 1999 3141
32. P.W. Codding J. Am. Chem. Soc. 105 1983 3172