HCV-P7 (Clarke et al., 2006). It's mechanism and function have been investigated in considerable detail (Gan et al. 2014). Histidine-17, which faces the lumen of the pore when protonated, allows Cl- entry, but deprotonation also allows Ca2+ entry. Imposition of voltage creates a Cl- current (Wang et al. 2014). The structure and dual pore/ion channel activity of p7 of different HCV genotypes have been reviewed (Madan and Bartenschlager 2015). It may transport protons; it's structure has been determined by NMR (Montserret et al. 2010) and by electron microscopy (Luik et al. 2009). The p7 N-terminal helical region is critical for
E2/p7 processing, protein-protein interactions, ion channel activity, and infectious HCV production (Scull et al. 2015). HCV p7 is released from the viral polyprotein through cleavage at E2-p7 and p7-NS2 junctions by signal peptidase, but also exists as an E2p7 precursor. The retarded E2p7 precursor cleavage is essential to regulate the intracellular and secreted levels of E2 through p7-mediated modulation of the cell secretory pathway (Denolly et al. 2017).
|Protein Name:||P7 aka Polyprotein|
|Species:||Hepatitis C virus subtype 1b  |
|Number of TMSs:||2|
|Location1 / Topology2 / Orientation3:
 “Hepatitis C Virus p7 membrane protein quasispecies variability in chronically infected patients treated with interferon and ribavirin, with or without amantadine.” Castelain S.et.al. 17177298
1: ALENLVVLNA ASLAGAHGIL SFLVFFCAAW YIKGRLVPGA AYAFYGVWPL LLLLLTLPPR