Document Detail


Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating.
MedLine Citation:
PMID:  22455917     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Loop-gating is one of two voltage-dependent mechanisms that regulate the open probability of connexin channels. The loop-gate permeability barrier is formed by a segment of the first extracellular loop (E1) (the parahelix) and appears to be accompanied by straightening of the bend angle between E1 and the first transmembrane domain (TM1). Here, all-atom molecular dynamics simulations are used to identify and characterize interacting van der Waals and electrostatic networks that stabilize the parahelices and TM1/E1 bend angles of the open Cx26 hemichannel. Dynamic fluctuations in an electrostatic network in each subunit are directly linked to the stability of parahelix structure and TM1/E1 bend angle in adjacent subunits. The electrostatic network includes charged residues that are pore-lining and thus positioned to be voltage sensors. We propose that the transition to the closed state is initiated by voltage-driven disruption of the networks that stabilize the open-state parahelix configuration, allowing the parahelix to protrude into the channel pore to form the loop-gate barrier. Straightening of the TM1/E1 bend appears to be a consequence of the reorganization of the interacting networks that accompany the conformational change of the parahelix. The electrostatic network extends across subunit boundaries, suggesting a concerted gating mechanism.
Authors:
Taekyung Kwon; Benoît Roux; Sunhwan Jo; Jeffery B Klauda; Andrew L Harris; Thaddeus A Bargiello
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-03-20
Journal Detail:
Title:  Biophysical journal     Volume:  102     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-03-29     Completed Date:  2012-08-02     Revised Date:  2013-05-20    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1341-51     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Affiliation:
Dominic P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution
Amino Acids / metabolism
Connexins / chemistry*,  metabolism*
Ion Channel Gating*
Ion Channels / chemistry*,  metabolism*
Molecular Dynamics Simulation*
Mutation / genetics
Permeability
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Subunits / chemistry,  metabolism
Static Electricity
Grant Support
ID/Acronym/Agency:
R01 GM062342/GM/NIGMS NIH HHS; R01 GM062342/GM/NIGMS NIH HHS; R01 GM064889/GM/NIGMS NIH HHS; R01 NS056509/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Connexins; 0/Ion Channels; 0/Protein Subunits; 127120-53-0/connexin 26
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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