Document Detail


Structure and function of the influenza A M2 proton channel.
MedLine Citation:
PMID:  19601584     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The M2 protein of influenza A viruses forms a tetrameric pH-activated proton-selective channel that is targeted by the amantadine class of antiviral drugs. Its ion channel function has been extensively studied by electrophysiology and mutagenesis; however, the molecular mechanism of proton transport is still elusive, and the mechanism of inhibition by amantadine is controversial. We review the functional data on proton channel activity, molecular dynamics simulations of the proton conduction mechanism, and high-resolution structural and dynamical information of this membrane protein in lipid bilayers and lipid-mimetic detergents. These studies indicate that elucidation of the structural basis of M2 channel activity and inhibition requires thorough examination of the complex dynamics and conformational plasticity of the protein in different lipid bilayers and lipid-mimetic environments.
Authors:
Sarah D Cady; Wenbin Luo; Fanghao Hu; Mei Hong
Related Documents :
1722254 - Identification of anion and cation pathways in the inner mitochondrial membrane by patc...
11526854 - The transport of salt and water across isolated rat ileum. evidence for at least two di...
7532434 - Non stochastic distribution of single channels in planar lipid bilayers.
12454924 - Early embryonic expression of ion channels and pumps in chick and xenopus development.
22417574 - Optimization of β-casein stabilized nanoemulsions using experimental mixture design.
24166894 - Charge carriers and small-polaron migration as the origin of intrinsic dielectric anoma...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemistry     Volume:  48     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-09-02     Completed Date:  2009-09-23     Revised Date:  2014-09-17    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7356-64     Citation Subset:  IM    
Data Bank Information
Bank Name/Acc. No.:
PDB/1NYJ;  2BKD;  2H95;  2KAD;  2RLF;  3C9J
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amantadine / chemistry
Amino Acid Sequence
Crystallography, X-Ray
Influenza A virus / chemistry*,  physiology
Ion Channels / antagonists & inhibitors,  chemistry*,  physiology
Lipid Bilayers / chemistry
Membrane Proteins / antagonists & inhibitors,  chemistry,  physiology
Molecular Sequence Data
Protein Conformation
Protein Structure, Tertiary
Protons*
Structure-Activity Relationship
Viral Matrix Proteins / antagonists & inhibitors,  chemistry*,  physiology
Grant Support
ID/Acronym/Agency:
R01 GM088204/GM/NIGMS NIH HHS; R01 GM088204-01/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Ion Channels; 0/Lipid Bilayers; 0/M2 protein, Influenza A virus; 0/Membrane Proteins; 0/Protons; 0/Viral Matrix Proteins; BF4C9Z1J53/Amantadine
Comments/Corrections

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


Previous Document:  The Photochemical C(2)-C(6) Cyclization of Enyne-Allenes: Interception of the Fulvene Diradical with...
Next Document:  Mechanistic investigations of the reaction of an iron(III) octa-anionic porphyrin complex with hydro...