1H-NMR signal assignments and secondary structure analysis of martentoxin.
J Asian Nat Prod Res
; 8(6): 511-8, 2006 Sep.
Article
em En
| MEDLINE
| ID: mdl-16931426
ABSTRACT
Martentoxin is a peptide of 37 amino acid residues purified from the venom of the Chinese scorpion Buthus martensi Karch, which has been demonstrated to be an inhibitor of voltage-dependent sodium channel and voltage-dependent delayed rectifier potassium channel. To elucidate the molecular mechanism of this interaction, the structure of martentoxin was studied by 2D-NMR. The secondary structure of martentoxin consists of a triple-stranded beta-sheet connected to a alpha-helical structure. This helix encompasses 10 residues from Ser11 to Lys20. The three strands of beta-sheet probably comprise residues Gly2-Asp5, Q27-N30 and Glu33-Cys36, Cys30-Asn33 with a type I'beta turn centered on Asn31-Asn32. The results indicate that martentoxin possesses the conserved beta alpha beta beta structure of all the potassium channel toxins.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Venenos de Escorpião
/
Escorpiões
Limite:
Animals
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article