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== Structure ==
== Structure ==
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NTCP is a transmembrane protein found in hepatocyte cells. It consists of nine <scene name='95/952697/Ntcp_open-pore_state/22'>transmembrane alpha helices</scene>, with the N-terminus located on the extracellular side of the plasma membrane and the C-terminus located on the intracellular side (Figure 3). Transmembrane helices are connected by short loops as well as extracellular and intracellular alpha helices that lie nearly parallel to the membrane.<ref name="Asami" /> Structures were determined by [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy (Cryo-EM)] of NTCP in complex with antibodies or nanobodies. <ref name="Goutam" /> <ref name="Asami" /> <Ref name="Park"> Park JH, Iwamoto M, Yun JH, Uchikubo-Kamo T, Son D, Jin Z, Yoshida H, Ohki M, Ishimoto N, Mizutani K, Oshima M, Muramatsu M, Wakita T, Shirouzu M, Liu K, Uemura T, Nomura N, Iwata S, Watashi K, Tame JRH, Nishizawa T, Lee W, Park SY. Structural insights into the HBV receptor and bile acid transporter NTCP. Nature. 2022 Jun;606(7916):1027-1031. [https://dx.doi.org/10.1038/s41586-022-04857-0 DOI: 10.1038/s41586-022-04857-0]. </Ref> <ref name="Liu" />
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NTCP is a transmembrane protein found in hepatocyte cells. It consists of nine <scene name='95/952697/Ntcp_open-pore_state/22'>transmembrane alpha helices</scene>, with the N-terminus located on the extracellular side of the plasma membrane and the C-terminus located on the intracellular side (Figure 3). The transmembrane helices are connected by short loops as well as extracellular and intracellular alpha helices that lie nearly parallel to the membrane.<ref name="Asami" /> Structures of NTCP were determined by [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy (Cryo-EM)] of NTCP in complex with antibodies or nanobodies. <ref name="Goutam" /> <ref name="Asami" /> <Ref name="Park"> Park JH, Iwamoto M, Yun JH, Uchikubo-Kamo T, Son D, Jin Z, Yoshida H, Ohki M, Ishimoto N, Mizutani K, Oshima M, Muramatsu M, Wakita T, Shirouzu M, Liu K, Uemura T, Nomura N, Iwata S, Watashi K, Tame JRH, Nishizawa T, Lee W, Park SY. Structural insights into the HBV receptor and bile acid transporter NTCP. Nature. 2022 Jun;606(7916):1027-1031. [https://dx.doi.org/10.1038/s41586-022-04857-0 DOI: 10.1038/s41586-022-04857-0]. </Ref> <ref name="Liu" />
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[[Image:Topology_picture.png|300 px|thumb|Figure 3. NTCP topology.]]
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[[Image:Topology_picture.png|300 px|thumb|Figure 3. NTCP topology. Transmembrane helices are numbered. TM helices comprising the panel domain are shown in orange. TM helices comprising the core domain are shown in shades of blue. Light and dark blue shades represent different helix bundles of the core domain, which together demonstrate pseudo two-fold symmetry.]]
=== Domains ===
=== Domains ===

Revision as of 13:24, 6 April 2023

Sodium-taurocholate Co-transporting Polypeptide

Sodium-taurocholate co-transporting Polypeptide (NTCP). The top is extracellular in relation to the hepatocyte, and the bottom is intracellular. Purple spheres represent Na+ ions and grey surfaces represent substrate. (PDB: 7ZYI)

Drag the structure with the mouse to rotate

References

  1. 1.0 1.1 1.2 1.3 Goutam K, Ielasi FS, Pardon E, Steyaert J, Reyes N. Structural basis of sodium-dependent bile salt uptake into the liver. Nature. 2022 Jun;606(7916):1015-1020. DOI: 10.1038/s41586-022-04723-z.
  2. 2.0 2.1 2.2 2.3 Asami J, Kimura KT, Fujita-Fujiharu Y, Ishida H, Zhang Z, Nomura Y, Liu K, Uemura T, Sato Y, Ono M, Yamamoto M, Noda T, Shigematsu H, Drew D, Iwata S, Shimizu T, Nomura N, Ohto U. Structure of the bile acid transporter and HBV receptor NTCP. Nature. 2022 Jun; 606 (7916):1021-1026. DOI: 10.1038/s41586-022-04845-4.
  3. 3.0 3.1 Park JH, Iwamoto M, Yun JH, Uchikubo-Kamo T, Son D, Jin Z, Yoshida H, Ohki M, Ishimoto N, Mizutani K, Oshima M, Muramatsu M, Wakita T, Shirouzu M, Liu K, Uemura T, Nomura N, Iwata S, Watashi K, Tame JRH, Nishizawa T, Lee W, Park SY. Structural insights into the HBV receptor and bile acid transporter NTCP. Nature. 2022 Jun;606(7916):1027-1031. DOI: 10.1038/s41586-022-04857-0.
  4. 4.0 4.1 4.2 Liu H, Irobalieva RN, Bang-Sørensen R, Nosol K, Mukherjee S, Agrawal P, Stieger B, Kossiakoff AA, Locher KP. Structure of human NTCP reveals the basis of recognition and sodium-driven transport of bile salts into the liver. Cell Res. 2022 Aug;32(8):773-776. DOI: 10.1038/s41422-022-00680-4.
  5. Qi X, Li W. Unlocking the secrets to human NTCP structure. Innovation (Camb). 2022 Aug 1;3(5):100294. DOI: 10.1016/j.xinn.2022.100294.
  6. 6.0 6.1 Zhang X, Zhang Q, Peng Q, Zhou J, Liao L, Sun X, Zhang L, Gong T. Hepatitis B virus preS1-derived lipopeptide functionalized liposomes for targeting of hepatic cells. Biomaterials. 2014 Jul;35(23):6130-41. DOI: 10.1016/j.biomaterials.2014.04.037.
  7. Patton JS, Carey MC. Watching fat digestion. Science. 1979 Apr 13;204(4389):145-8. DOI: 10.1126/science.432636.
  8. Donkers JM, Kooijman S, Slijepcevic D, Kunst RF, Roscam Abbing RL, Haazen L, de Waart DR, Levels JH, Schoonjans K, Rensen PC, Oude Elferink RP, van de Graaf SF. NTCP deficiency in mice protects against obesity and hepatosteatosis. JCI Insight. 2019 Jun 25;5(14):e127197. DOI: 10.1172/jci.insight.127197.

Student Contributors

  • Ben Minor
  • Maggie Samm
  • Zac Stanley
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