Sandbox Reserved 1769: Difference between revisions

Bile salts recognize and bind to the <scene name='95/952697/Ntcp_open-pore_state_surface/1'>open-pore state</scene>. After binding, bile salts pass through the amphipathic pore and NTCP transitions into the <scene name='95/952697/Ntcp_inward_facing_state/1'>inward facing state</scene>. In this conformation, the pore once open to the extracellular side is now closed and is now open to the cytoplasmic side. Transition to the inward facing state allows release of bile salts and sodium ions. It is not yet known how this transition exactly proceeds.  

The HBV/HDV capsid must be myristoylated (INSERT BLUE LINK) in order for proper recognition by NTCP. Residues 2-48 are the most significant residues of HBV/HDV that are highly conserved amongst these viruses that are vital for infection. Specifically, residues 8-17 on HBV/HDV have been identified as the most important. These residues are NPLGFFPDHQ. There are two proposed mechanisms as to how exactly HBV/HDV bind to NTCP and enter the cell. In both mechanisms, there is an initial translocation of the myristoylated preS1 HBV/HDV virus to interact with the host cell (hepatocyte). The first mechanism involves the myristoyl group of preS1 binding to the host cell membrane, not NTCP, and residues P8-H17 interacting with NTCP residues 157-165. The second mechanism involves the myristoyl group of preS1 binding directly into the open-pore of NTCP interacting with residues 157-165. In both proposed mechanisms, the interactions with the extracellular residues 84-87 of NTCP is unknown.