ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.
Identifieur interne : 002190 ( Ncbi/Curation ); précédent : 002189; suivant : 002191ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.
Auteurs : Cheng-Chang Chen [Taïwan] ; Jens Krüger ; Issara Sramala ; Hao-Jen Hsu ; Peter Henklein ; Yi-Ming Arthur Chen ; Wolfgang B. FischerSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2011.
Descripteurs français
- KwdFr :
- Canaux ioniques (), Canaux ioniques (génétique), Données de séquences moléculaires, Double couche lipidique, Modèles moléculaires, Protéines de la matrice virale (), Protéines de la matrice virale (génétique), Simulation de dynamique moléculaire, Simulation numérique, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS (), Virus du SRAS (génétique).
- MESH :
- génétique : Canaux ioniques, Protéines de la matrice virale, Virus du SRAS.
- Canaux ioniques, Données de séquences moléculaires, Double couche lipidique, Modèles moléculaires, Protéines de la matrice virale, Simulation de dynamique moléculaire, Simulation numérique, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS.
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
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pubmed:20708597Le document en format XML
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Fischer</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Computer Simulation</term><term>Ion Channels (chemistry)</term><term>Ion Channels (genetics)</term><term>Lipid Bilayers</term><term>Models, Molecular</term><term>Molecular Dynamics Simulation</term><term>Molecular Sequence Data</term><term>Protein Structure, Secondary</term><term>SARS Virus (chemistry)</term><term>SARS Virus (genetics)</term><term>Viral Matrix Proteins (chemistry)</term><term>Viral Matrix Proteins (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Canaux ioniques ()</term><term>Canaux ioniques (génétique)</term><term>Données de séquences moléculaires</term><term>Double couche lipidique</term><term>Modèles moléculaires</term><term>Protéines de la matrice virale ()</term><term>Protéines de la matrice virale (génétique)</term><term>Simulation de dynamique moléculaire</term><term>Simulation numérique</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS ()</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ion Channels</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ion Channels</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Canaux ioniques</term><term>Protéines de la matrice virale</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Computer Simulation</term><term>Lipid Bilayers</term><term>Models, Molecular</term><term>Molecular Dynamics Simulation</term><term>Molecular Sequence Data</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Canaux ioniques</term><term>Données de séquences moléculaires</term><term>Double couche lipidique</term><term>Modèles moléculaires</term><term>Protéines de la matrice virale</term><term>Simulation de dynamique moléculaire</term><term>Simulation numérique</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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