EMD-34982

Single-particle
3.11 Å
EMD-34982 Deposition: 16/12/2022
Map released: 17/01/2024
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-34982

Cryo-EM structure of human NTCP-myr-preS1-YN9016Fab complex

EMD-34982

Single-particle
3.11 Å
EMD-34982 Deposition: 16/12/2022
Map released: 17/01/2024
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens, Ondatra zibethicus, Hepatitis B virus
Sample: NTCP-myr-preS1-YN9016Fab
Fitted models: 8hry (Avg. Q-score: 0.523)

Deposition Authors: Asami J, Shimizu T , Ohto U
Structural basis of hepatitis B virus receptor binding.
PUBMED: 38233573
DOI: doi:10.1038/s41594-023-01191-5
ISSN: 1545-9985
Abstract:
Hepatitis B virus (HBV), a leading cause of developing hepatocellular carcinoma affecting more than 290 million people worldwide, is an enveloped DNA virus specifically infecting hepatocytes. Myristoylated preS1 domain of the HBV large surface protein binds to the host receptor sodium-taurocholate cotransporting polypeptide (NTCP), a hepatocellular bile acid transporter, to initiate viral entry. Here, we report the cryogenic-electron microscopy structure of the myristoylated preS1 (residues 2-48) peptide bound to human NTCP. The unexpectedly folded N-terminal half of the peptide embeds deeply into the outward-facing tunnel of NTCP, whereas the C-terminal half formed extensive contacts on the extracellular surface. Our findings reveal an unprecedented induced-fit mechanism for establishing high-affinity virus-host attachment and provide a blueprint for the rational design of anti-HBV drugs targeting virus entry.