ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.
Identifieur interne : 001649 ( PubMed/Corpus ); précédent : 001648; suivant : 001650ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.
Auteurs : Cheng-Chang Chen ; Jens Krüger ; Issara Sramala ; Hao-Jen Hsu ; Peter Henklein ; Yi-Ming Arthur Chen ; Wolfgang B. FischerSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2011.
English descriptors
- KwdEn :
- Amino Acid Sequence, Computer Simulation, Ion Channels (chemistry), Ion Channels (genetics), Lipid Bilayers, Models, Molecular, Molecular Dynamics Simulation, Molecular Sequence Data, Protein Structure, Secondary, SARS Virus (chemistry), SARS Virus (genetics), Viral Matrix Proteins (chemistry), Viral Matrix Proteins (genetics).
- MESH :
- chemical , chemistry : Ion Channels, Viral Matrix Proteins.
- chemical , genetics : Ion Channels, Viral Matrix Proteins.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- Amino Acid Sequence, Computer Simulation, Lipid Bilayers, Models, Molecular, Molecular Dynamics Simulation, Molecular Sequence Data, Protein Structure, Secondary.
Abstract
ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9±0.8pS at elevated temperature (38.5°C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.
DOI: 10.1016/j.bbamem.2010.08.004
PubMed: 20708597
Links to Exploration step
pubmed:20708597Le document en format XML
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<front><div type="abstract" xml:lang="en">ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9±0.8pS at elevated temperature (38.5°C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.</div>
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<Abstract><AbstractText>ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9±0.8pS at elevated temperature (38.5°C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.</AbstractText>
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