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TitleStructure of the bile acid transporter and HBV receptor NTCP.
Journal, issue, pagesNature, Vol. 606, Issue 7916, Page 1021-1026, Year 2022
Publish dateMay 17, 2022
AuthorsJinta Asami / Kanako Terakado Kimura / Yoko Fujita-Fujiharu / Hanako Ishida / Zhikuan Zhang / Yayoi Nomura / Kehong Liu / Tomoko Uemura / Yumi Sato / Masatsugu Ono / Masaki Yamamoto / Takeshi Noda / Hideki Shigematsu / David Drew / So Iwata / Toshiyuki Shimizu / Norimichi Nomura / Umeharu Ohto /
PubMed AbstractChronic infection with hepatitis B virus (HBV) affects more than 290 million people worldwide, is a major cause of cirrhosis and hepatocellular carcinoma, and results in an estimated 820,000 deaths ...Chronic infection with hepatitis B virus (HBV) affects more than 290 million people worldwide, is a major cause of cirrhosis and hepatocellular carcinoma, and results in an estimated 820,000 deaths annually. For HBV infection to be established, a molecular interaction is required between the large glycoproteins of the virus envelope (known as LHBs) and the host entry receptor sodium taurocholate co-transporting polypeptide (NTCP), a sodium-dependent bile acid transporter from the blood to hepatocytes. However, the molecular basis for the virus-transporter interaction is poorly understood. Here we report the cryo-electron microscopy structures of human, bovine and rat NTCPs in the apo state, which reveal the presence of a tunnel across the membrane and a possible transport route for the substrate. Moreover, the cryo-electron microscopy structure of human NTCP in the presence of the myristoylated preS1 domain of LHBs, together with mutation and transport assays, suggest a binding mode in which preS1 and the substrate compete for the extracellular opening of the tunnel in NTCP. Our preS1 domain interaction analysis enables a mechanistic interpretation of naturally occurring HBV-insusceptible mutations in human NTCP. Together, our findings provide a structural framework for HBV recognition and a mechanistic understanding of sodium-dependent bile acid translocation by mammalian NTCPs.
External linksNature / PubMed:35580629
MethodsEM (single particle)
Resolution3.11 - 3.55 Å
Structure data

31837

7vad

EMDB-31837, PDB-7vad:
Cryo-EM structure of human NTCP complexed with YN69202Fab
Method: EM (single particle) / Resolution: 3.41 Å

31838

7vae

EMDB-31838, PDB-7vae:
Cryo-EM structure of bovine NTCP complexed with YN69202Fab
Method: EM (single particle) / Resolution: 3.55 Å

31839

7vaf

EMDB-31839, PDB-7vaf:
Cryo-EM structure of Rat NTCP complexed with YN69202Fab
Method: EM (single particle) / Resolution: 3.11 Å

31840

7vag

EMDB-31840, PDB-7vag:
Cryo-EM structure of human NTCP complexed with YN69202Fab in the presence of myristoylated preS1 peptide
Method: EM (single particle) / Resolution: 3.32 Å

32759

7wsi

EMDB-32759, PDB-7wsi:
Cryo-EM structure of human NTCP (wild-type) complexed with YN69202Fab
Method: EM (single particle) / Resolution: 3.32 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • bos taurus (cattle)
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / Hepatitis B virus (HBV) / host entry receptor / bile acid transporter / taurocholate / Na+-coupled symporter

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