Sandbox Reserved 1793: Difference between revisions

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A proposed pathway for NTCP bile salt transport starting and ending with open-pore states hypothesizes that both sodium ions are translocated with the transport of one bile salt.<Ref name = "Liu"> Liu, H., Irobalieva, R.N., Bang-Sørensen, R. et al. Structure of human NTCP reveals the basis of recognition and sodium-driven transport of bile salts into the liver. Cell Res 32, 773–776 (2022). https://doi.org/10.1038/s41422-022-00680-4 </Ref>. Only one taurocholate is transported at a time due to NTCP's two bile salt binding sites. An

<scene name='95/952721/Inner_bile_salt/2'>inner bile salt</scene> that is closer to the cytoplasmic side of the membrane and an <scene name='95/952721/Outer_bile_salt/2'>outer bile salt</scene> that is closer to the extracellular side of the membrane <Ref name = "Liu"/> In the open-pore state both <scene name='95/952721/Mech_step_1/1'>taurocholates and sodium ions bound</scene> then both sodium ions are released into the cytoplasm along with the inner bile salt into the cytoplasm (Fig. 5). The <scene name='95/952721/Mech_step_2/2'>outermost bile salt remains bound</scene> in the pore, likely helping to prevent leakage. <Ref name = "Liu"/> The <scene name='95/952721/Mech_step_3/2'> outer bile salt is displaced </scene> into the inner bile salt binding site by the movement of sodium ions, this displacement then facilitates the conformational change to the inward-facing, pore inaccessible conformation (Fig. 5). <Ref name = "Liu"/> Sodium ions then bind to NTCP, favoring the open-pore state and also allowing for the binding of another outer bile salt (Fig 5). The <scene name='95/952721/Mech_step_1/1'>protein is then reset</scene> and the process can then start again releasing the next inner bile salt with the translocation of the sodium ions into the cytoplasm. This mechanism melds typical patterns of ~~gated ion channels and~~ [https://proteopedia.org/wiki/index.php/Pump pumps] in a new light as sodium ions control conformation and thus binding, displacement, and release of bile salts. <Ref name = "Goutam"/>

<scene name='95/952721/Inner_bile_salt/2'>inner bile salt</scene> that is closer to the cytoplasmic side of the membrane and an <scene name='95/952721/Outer_bile_salt/2'>outer bile salt</scene> that is closer to the extracellular side of the membrane <Ref name = "Liu"/> In the open-pore state both <scene name='95/952721/Mech_step_1/1'>taurocholates and sodium ions bound</scene> then both sodium ions are released into the cytoplasm along with the inner bile salt into the cytoplasm (Fig. 5). The <scene name='95/952721/Mech_step_2/2'>outermost bile salt remains bound</scene> in the pore, likely helping to prevent leakage. <Ref name = "Liu"/> The <scene name='95/952721/Mech_step_3/2'> outer bile salt is displaced </scene> into the inner bile salt binding site by the movement of sodium ions, this displacement then facilitates the conformational change to the inward-facing, pore inaccessible conformation (Fig. 5). <Ref name = "Liu"/> Sodium ions then bind to NTCP, favoring the open-pore state and also allowing for the binding of another outer bile salt (Fig 5). The <scene name='95/952721/Mech_step_1/1'>protein is then reset</scene> and the process can then start again releasing the next inner bile salt with the translocation of the sodium ions into the cytoplasm. This mechanism melds typical patterns of [https://proteopedia.org/wiki/index.php/Pump gated channels and pumps] in a new light as sodium ions control conformation and thus binding, displacement, and release of bile salts. <Ref name = "Goutam"/>

== HBV Binding and Infection==

Sandbox Reserved 1793: Difference between revisions

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@@ Line 35: / Line 35: @@
 A proposed pathway for NTCP bile salt transport starting and ending with open-pore states hypothesizes that both sodium ions are translocated with the transport of one bile salt.<Ref name = "Liu"> Liu, H., Irobalieva, R.N., Bang-Sørensen, R. et al. Structure of human NTCP reveals the basis of recognition and sodium-driven transport of bile salts into the liver. Cell Res 32, 773–776 (2022). https://doi.org/10.1038/s41422-022-00680-4 </Ref>. Only one taurocholate is transported at a time due to NTCP's two bile salt binding sites. An
-<scene name='95/952721/Inner_bile_salt/2'>inner bile salt</scene> that is closer to the cytoplasmic side of the membrane and an <scene name='95/952721/Outer_bile_salt/2'>outer bile salt</scene> that is closer to the extracellular side of the membrane <Ref name = "Liu"/> In the open-pore state both <scene name='95/952721/Mech_step_1/1'>taurocholates and sodium ions bound</scene> then both sodium ions are released into the cytoplasm along with the inner bile salt into the cytoplasm (Fig. 5). The <scene name='95/952721/Mech_step_2/2'>outermost bile salt remains bound</scene> in the pore, likely helping to prevent leakage. <Ref name = "Liu"/> The <scene name='95/952721/Mech_step_3/2'> outer bile salt is displaced </scene> into the inner bile salt binding site by the movement of sodium ions, this displacement then facilitates the conformational change to the inward-facing, pore inaccessible conformation (Fig. 5). <Ref name = "Liu"/> Sodium ions then bind to NTCP, favoring the open-pore state and also allowing for the binding of another outer bile salt (Fig 5). The <scene name='95/952721/Mech_step_1/1'>protein is then reset</scene> and the process can then start again releasing the next inner bile salt with the translocation of the sodium ions into the cytoplasm. This mechanism melds typical patterns of gated ion channels and [https://proteopedia.org/wiki/index.php/Pump pumps] in a new light as sodium ions control conformation and thus binding, displacement, and release of bile salts. <Ref name = "Goutam"/>
+<scene name='95/952721/Inner_bile_salt/2'>inner bile salt</scene> that is closer to the cytoplasmic side of the membrane and an <scene name='95/952721/Outer_bile_salt/2'>outer bile salt</scene> that is closer to the extracellular side of the membrane <Ref name = "Liu"/> In the open-pore state both <scene name='95/952721/Mech_step_1/1'>taurocholates and sodium ions bound</scene> then both sodium ions are released into the cytoplasm along with the inner bile salt into the cytoplasm (Fig. 5). The <scene name='95/952721/Mech_step_2/2'>outermost bile salt remains bound</scene> in the pore, likely helping to prevent leakage. <Ref name = "Liu"/> The <scene name='95/952721/Mech_step_3/2'> outer bile salt is displaced </scene> into the inner bile salt binding site by the movement of sodium ions, this displacement then facilitates the conformational change to the inward-facing, pore inaccessible conformation (Fig. 5). <Ref name = "Liu"/> Sodium ions then bind to NTCP, favoring the open-pore state and also allowing for the binding of another outer bile salt (Fig 5). The <scene name='95/952721/Mech_step_1/1'>protein is then reset</scene> and the process can then start again releasing the next inner bile salt with the translocation of the sodium ions into the cytoplasm. This mechanism melds typical patterns of [https://proteopedia.org/wiki/index.php/Pump gated channels and pumps] in a new light as sodium ions control conformation and thus binding, displacement, and release of bile salts. <Ref name = "Goutam"/>
 == HBV Binding and Infection==