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Journal of Asian Natural Products Research Volume 8, 2006 - Issue 6
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Original Articles

1H-NMR signal assignments and secondary structure analysis of martentoxin

Y.-H. WANG Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, Beijing, 100050, China
,
Z.-Y. CAO Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, Beijing, 100050, China
,
W.-Y. HE Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, Beijing, 100050, China
,
X.-Z. YAN Academy of Military Medical Sciences, National Center of Biomedical Analysis, Institute of Toxicology and Pharmacology, Beijing, 100850, China
,
X. LIU Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, Beijing, 100050, China
,
H.-Y. LIU Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, Beijing, 100050, China
,
X.-T. LIANG Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, Beijing, 100050, China
&
D.-Q. YU Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, Beijing, 100050, ChinaCorrespondence[email protected]
 show all
Pages 511-518 | Received 10 Nov 2004, Accepted 23 Dec 2004, Published online: 17 Dec 2010
 
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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 β-sheet connected to a α-helical structure. This helix encompasses 10 residues from Ser11 to Lys20. The three strands of β-sheet probably comprise residues Gly2-Asp5, Q27-N30 and Glu33-Cys36, Cys30-Asn33 with a type I′β turn centered on Asn31-Asn32. The results indicate that martentoxin possesses the conserved β α β β structure of all the potassium channel toxins.

Acknowledgements

The authors are thankful to Dr. Guang-Zhong Tu of Beijing Institute of Microchemistry and Dr. Huai-Reng Huang of the Institute of Biophysics, Chinese Academy of Sciences for technical assistance.

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