Sandbox Reserved 1769: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
== Structure == | == Structure == | ||
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, which served to stabilize two known conformational states of NTCP. <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" /> These complexed antibodies/nanobodies have been removed from all structures shown on this page. | 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 [https://en.wikipedia.org/wiki/Antibody antibodies] or [https://en.wikipedia.org/wiki/Single-domain_antibody nanobodies], which served to stabilize two known conformational states of NTCP. <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" /> These complexed antibodies/nanobodies have been removed from all structures shown on this page. | ||
[[Image:Topology_picture.png|300 px|thumb|Figure 3. NTCP topology. Transmembrane helices are numbered. The panel domain is shown in orange. The core domain is shown in two shades of blue. Light and dark blue shades represent different helix bundles of the core domain, which together demonstrate pseudo two-fold symmetry.]] | [[Image:Topology_picture.png|300 px|thumb|Figure 3. NTCP topology. Transmembrane helices are numbered. The panel domain is shown in orange. The core domain is shown in two shades of blue. Light and dark blue shades represent different helix bundles of the core domain, which together demonstrate pseudo two-fold symmetry.]] | ||