Sandbox Reserved 1769: Difference between revisions
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=== Domains === | === Domains === | ||
NTCP contains <scene name='95/952697/Ntcp_open-pore_state/21'>two characteristic domains</scene>: the core and panel domains (Figure 3). Movement of these two domains allows recognition and transport of bile acids into hepatocytes. | NTCP contains <scene name='95/952697/Ntcp_open-pore_state/21'>two characteristic domains</scene>: the core and panel domains (Figure 3). Movement of these two domains allows recognition and transport of bile acids into hepatocytes. | ||
*<b><font color="orange">Panel Domain</font></b>: <scene name='95/952697/Ntcp_open-pore_state/ | *<b><font color="orange">Panel Domain</font></b>: <scene name='95/952697/Ntcp_open-pore_state/23'>Residues 1-44, 155-208</scene> | ||
** Formed by transmembrane helices TM1, TM5, and TM6. | ** Formed by transmembrane helices TM1, TM5, and TM6. | ||
*<b><font color="#0040e0">Core domain</font></b>: <scene name='95/952697/Ntcp_open-pore_state/ | *<b><font color="#0040e0">Core domain</font></b>: <scene name='95/952697/Ntcp_open-pore_state/24'>Residues 45-154, 209-309</scene> | ||
**Formed by the packing of a helix bundle of <b><font color="blue">TM2, TM3, and TM4</font></b> with another helix bundle of <b><font color="skyblue">TM7, TM8, and TM9</font></b>. These two helix bundles are related by pseudo two-fold symmetry.<Ref name="Qi"> Qi X, Li W. Unlocking the secrets to human NTCP structure. Innovation (Camb). 2022 Aug 1;3(5):100294. [https://dx.doi.org/10.1016/j.xinn.2022.100294 DOI: 10.1016/j.xinn.2022.100294]. </Ref> | **Formed by the packing of a helix bundle of <b><font color="blue">TM2, TM3, and TM4</font></b> with another helix bundle of <b><font color="skyblue">TM7, TM8, and TM9</font></b>. These two helix bundles are related by pseudo two-fold symmetry.<Ref name="Qi"> Qi X, Li W. Unlocking the secrets to human NTCP structure. Innovation (Camb). 2022 Aug 1;3(5):100294. [https://dx.doi.org/10.1016/j.xinn.2022.100294 DOI: 10.1016/j.xinn.2022.100294]. </Ref> | ||
=== Proline/Glycine Hinge === | === Proline/Glycine Hinge === | ||
<scene name='95/952697/Ntcp_open-pore_state/ | <scene name='95/952697/Ntcp_open-pore_state/25'>Glycine and proline residues</scene> in the connecting loops and extra- and intracellular helices (Figure 3) act as hinges in the mechanism of bile salt uptake. This flexibility allows separation of the core and panel domains, creating a pore open to the extracellular space and exposing critical Na+ binding sites. Once substrate binds the open-pore state, this hinge allows the transition to close this pore relative to the extracellular side and open to the cytoplasmic side, thus allowing release of substrate into the cell.<ref name = "Goutam" /> | ||
=== Sodium Binding Sites === | === Sodium Binding Sites === | ||
