The Role of Individual Disulfide Bonds of μ-Conotoxin GIIIA in the Inhibition of NaV1.4

The Role of Individual Disulfide Bonds of μ-Conotoxin GIIIA in the Inhibition of NaV1.4

μ-Conotoxin GIIIA, a peptide toxin isolated from Conus geographus, preferentially blocks the skeletal muscle sodium channel NaV1.4. GIIIA folds compactly to a pyramidal structure stabilized by three disulfide bonds. To assess the contributions of individual disulfide bonds of GIIIA to the blockade o...

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Bibliographic Details
Main Authors: Penggang Han, Kang Wang, Xiandong Dai, Ying Cao, Shangyi Liu, Hui Jiang, Chongxu Fan, Wenjian Wu, Jisheng Chen
Format: Article
Language:English
Published: MDPI AG 2016-11-01
Series:Marine Drugs
Subjects:
μ-conotoxin
GIIIA
disulfide bond
NaV1.4
electrophysiology
Online Access:http://www.mdpi.com/1660-3397/14/11/213

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http://www.mdpi.com/1660-3397/14/11/213

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