کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5370976 | 1503924 | 2014 | 8 صفحه PDF | دانلود رایگان |
- Generation of hexameric assemblies of ion channel forming p7 of HCV
- Protonation of His-17 allows Cl-ions to enter the pore.
- In unprotonated bundle also Ca-ions are found within the pore.
- Applied voltage identifies large Cl-ion currents from the site of the loop.
- Slight rectification of the current is observed.
Viral proteins assemble into homopolymers in the infected cells and have a role as diffusion-amplifier for ions across subcellular membranes. The homopolymer of hepatitis C virus, protein p7 of strain 1a, which is known to form channels, is used to investigate the dynamics of physiological relevant ions, Na+, K+, Clâ and Ca2+ in the vicinity of the protein bundle. The protein bundle is generated by a combination of docking approach and molecular dynamics (MD) simulations. Ion dynamics are recorded during multiple 200Â ns MD simulations of 1Â M solutions. His-17 is found to point into the lumen of the pore. Protonation of this residue allows Cl-ions to enter the pore while in its unprotonated state Ca-ions are found within the pore as well. Applied voltage identifies large Cl-ion currents from the site of the loop passing through the pore. Rectification of the current of the Cl-ions is observed.
Journal: Biophysical Chemistry - Volume 192, August 2014, Pages 33-40