Structural basis of sodium-dependent bile salt uptake into the liver.

ABSTRACT: The liver takes up bile salts from blood to generate bile, enabling absorption of lipophilic nutrients and excretion of metabolites and drugs¹. Human Na⁺-taurocholate co-transporting polypeptide (NTCP) is the main bile salt uptake system in liver. NTCP is also the cellular entry receptor of human hepatitis B and D viruses^2,3 (HBV/HDV), and has emerged as an important target for antiviral drugs⁴. However, the molecular mechanisms underlying NTCP transport and viral receptor functions remain incompletely understood. Here we present cryo-electron microscopy structures of human NTCP in complexes with nanobodies, revealing key conformations of its transport cycle. NTCP undergoes a conformational transition opening a wide transmembrane pore that serves

SUBMITTER: Goutam K 

PROVIDER: S-EPMC9242856 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature