Unknown

Dataset Information

0

ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.


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.

SUBMITTER: Chen CC 

PROVIDER: S-EPMC7094593 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.

Chen Cheng-Chang CC   Krüger Jens J   Sramala Issara I   Hsu Hao-Jen HJ   Henklein Peter P   Chen Yi-Ming Arthur YM   Fischer Wolfgang B WB  

Biochimica et biophysica acta 20100812 2


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 putativ  ...[more]

Similar Datasets

| S-EPMC9250420 | biostudies-literature
| S-EPMC6695816 | biostudies-literature
| S-EPMC7663461 | biostudies-literature
| S-EPMC9578647 | biostudies-literature
| S-EPMC9820416 | biostudies-literature
| S-EPMC3107394 | biostudies-literature
| S-EPMC1300661 | biostudies-other
| S-EPMC9874072 | biostudies-literature
| S-EPMC9636605 | biostudies-literature
| S-EPMC9469804 | biostudies-literature