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Conserved functional surface of antimammalian scorpion β-toxins

Date

Authors

Chen, Rong

Chung, Shin-Ho

Publisher

American Chemical Society

Abstract

Scorpion β-toxins bind to the voltage-sensing domain of voltage-gated sodium (NaV) channels and trap the voltage-sensing domain in the activated state. Two structurally similar β-toxins from scorpions, Css4 and Cn2, selectively target different subtypes

Keywords

Keywords: Binding modes; Charged residues; Dissociation constant; Functional surfaces; Molecular docking; Molecular dynamics simulations; Receptor sites; Umbrella sampling; Binding energy; Dissociation; Mammals; Metabolites; Molecular dynamics; Sodium; Toxic materi

URI

http://hdl.handle.net/1885/64164

Collections

ANU Research Publications

Source

Journal of Physical Chemistry B

Type

Journal article

DOI

10.1021/jp300127j

Restricted until

2037-12-31

Downloads

File

Description

01_Chen_Conserved_functional_surface_2012.pdf (1.97 MB)