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Conserved functional surface of antimammalian scorpion β-toxins

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Chen, Rong; Chung, Shin-Ho

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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

dc.contributor.authorChen, Rong
dc.contributor.authorChung, Shin-Ho
dc.date.accessioned2015-12-10T23:12:52Z
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/1885/64164
dc.description.abstractScorpion 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
dc.publisherAmerican Chemical Society
dc.sourceJournal of Physical Chemistry B
dc.subjectKeywords: 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
dc.titleConserved functional surface of antimammalian scorpion β-toxins
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume116
dc.date.issued2012
local.identifier.absfor030600 - PHYSICAL CHEMISTRY (INCL. STRUCTURAL)
local.identifier.ariespublicationf5625xPUB896
local.type.statusPublished Version
local.contributor.affiliationChen, Rong, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationChung, Shin-Ho, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue16
local.bibliographicCitation.startpage4796
local.bibliographicCitation.lastpage4800
local.identifier.doi10.1021/jp300127j
dc.date.updated2016-02-24T09:44:37Z
local.identifier.scopusID2-s2.0-84860267724
local.identifier.thomsonID000303173800008
CollectionsANU Research Publications

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