Ion-dynamics in hepatitis C virus p7 helical transmembrane domains

• Verfasst von: Wang, Yi-Ting [VerfasserIn]
• Verfasst von: Schilling, Roman [VerfasserIn]
• Verfasst von: Fink, Rainer [VerfasserIn]
• Verfasst von: Fischer, Wolfgang B. [VerfasserIn]
• Titel: Ion-dynamics in hepatitis C virus p7 helical transmembrane domains
• Titelzusatz: a molecular dynamics simulation study
• Verf.angabe: Yi-Ting Wang, Roman Schilling, Rainer H.A. Fink, Wolfgang B. Fischer
• E-Jahr: 2014
• Jahr: 16 June 2014
• Umfang: 8 S.
• Fussnoten: Gesehen am 03.09.2020
• Titel Quelle: Enthalten in: Biophysical chemistry
• Ort Quelle: Amsterdam [u.a.] : Elsevier Science, 1973
• Jahr Quelle: 2014
• Band/Heft Quelle: 192(2014), Seite 33-40
• ISSN Quelle: 1873-4200
• DOI: doi:10.1016/j.bpc.2014.06.001
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Computational modeling
• Sach-SW: Conductance
• Sach-SW: Ion channels
• Sach-SW: Membrane protein
• Sach-SW: Protein structure
• K10plus-PPN: 1728768306

Abstract

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+, Cl− 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 200ns MD simulations of 1M 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.