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TitleStructure of nanobody-inhibited state of human bile salt transporter NTCP.
Journal, issue, pagesStructure, Year 2025
Publish dateOct 24, 2025
AuthorsDaniel Yoon / Kamil Nosol / Ali Rasouli / Rose Bang-Sørensen / Rossitza N Irobalieva / Hongtao Liu / Emad Tajkhorshid / Kaspar P Locher /
PubMed AbstractSodium-taurocholate co-transporting polypeptide (NTCP) is a sodium-dependent transporter mediating the hepatic uptake of bile salts and serving as the receptor of hepatitis B and D viruses. While ...Sodium-taurocholate co-transporting polypeptide (NTCP) is a sodium-dependent transporter mediating the hepatic uptake of bile salts and serving as the receptor of hepatitis B and D viruses. While previous studies identified binding sites for sodium ions and substrates, the mechanism remains controversial. We here report a high-resolution structure of NTCP in a closed-tunnel conformation that does not feature substrate binding sites but reveals evidence of two bound sodium ions. To evaluate the functional relevance of this state and gain insight into the transport mechanism, we performed μs-scale molecular dynamics simulations of NTCP starting from distinct conformations and substrate and ion configurations. We observed that both the closed-tunnel and open-tunnel conformations are highly stable, but that the sodium ions and bile salt molecules can shift positions without substantial conformational changes. Our results suggest that the closed-tunnel conformation might represents an inactive state rather than an essential component of a productive transport cycle.
External linksStructure / PubMed:41138719
MethodsEM (single particle)
Resolution3.11 Å
Structure data

53474

9qzq

EMDB-53474, PDB-9qzq:
CryoEM structure of nanodisc-reconstituted human NTCP in complex with grafted NTCP_Nb1 and NabFab
Method: EM (single particle) / Resolution: 3.11 Å

Chemicals

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
  • vicugna pacos (alpaca)
KeywordsTRANSPORT PROTEIN / Solute Carrier Protein / Bile salt transporter / HBV/ HDV receptor / Sodium-coupled transport

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