Sandbox Reserved 1794: Difference between revisions

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==== Bile Salts ====

A key feature of NTCP is its <scene name='95/~~952721~~/Amphipathic_patterns/2'>amphipathic pore</scene> which allows for bile salt transport across the hydrophilic membrane. The pore surface remains {{Template:ColorKey_Hydrophobic}}, while the <scene name='95/952721/Amphipathic_patterns_pore/2'>lining of the open pore</scene> is largely {{Template:ColorKey_Polar}}. In the inward-facing or closed-pore conformation, the polar pore residues are inaccessible. Only the surface hydrophobic residues are exposed. As the pore opens up, inner polar residues become accessible allowing for the binding of hydrophilic bile salts. The pattern of hydrophobic and polar residues within the pore matches the amphipathic patterns within taurocholates, [https://en.wikipedia.org/wiki/Steroid steroids], and [https://en.wikipedia.org/wiki/Thyroid_hormones thyroid hormones]. <Ref name = Qi> Qi X. and Li W. (2022). Unlocking the secrets to human NTCP structure. The Innovation 3(5), 100294. https://doi.org/10.1016/j.xinn.2022.100294 </ref> Using this amphipathic pore, provides the channel with specificity while preventing leakage of other substrates. Essential <scene name='95/952722/Bile_salts_res/1'>bile salt binding residues</scene> form Van der Waals interactions with bile salt substrates, while others form dipole-dipole or ionic interactions. The core domain contributes most of the polar domains, while the panel domain contributes mainly hydrophobic surface.

A key feature of NTCP is its <scene name='95/952722/Amphipathic_patterns/1'>amphipathic pore</scene> which allows for bile salt transport across the hydrophilic membrane. The pore surface remains {{Template:ColorKey_Hydrophobic}}, while the <scene name='95/952721/Amphipathic_patterns_pore/2'>lining of the open pore</scene> is largely {{Template:ColorKey_Polar}}. In the inward-facing or closed-pore conformation, the polar pore residues are inaccessible. Only the surface hydrophobic residues are exposed. As the pore opens up, inner polar residues become accessible allowing for the binding of hydrophilic bile salts. The pattern of hydrophobic and polar residues within the pore matches the amphipathic patterns within taurocholates, [https://en.wikipedia.org/wiki/Steroid steroids], and [https://en.wikipedia.org/wiki/Thyroid_hormones thyroid hormones]. <Ref name = Qi> Qi X. and Li W. (2022). Unlocking the secrets to human NTCP structure. The Innovation 3(5), 100294. https://doi.org/10.1016/j.xinn.2022.100294 </ref> Using this amphipathic pore, provides the channel with specificity while preventing leakage of other substrates. Essential <scene name='95/952722/Bile_salts_res/1'>bile salt binding residues</scene> form Van der Waals interactions with bile salt substrates, while others form dipole-dipole or ionic interactions. The core domain contributes most of the polar domains, while the panel domain contributes mainly hydrophobic surface.

=== Conformational Change ===

Sandbox Reserved 1794: Difference between revisions

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 ==== Bile Salts ====
-A key feature of NTCP is its <scene name='95/952721/Amphipathic_patterns/2'>amphipathic pore</scene> which allows for bile salt transport across the hydrophilic membrane. The pore surface remains {{Template:ColorKey_Hydrophobic}}, while the <scene name='95/952721/Amphipathic_patterns_pore/2'>lining of the open pore</scene> is largely {{Template:ColorKey_Polar}}. In the inward-facing or closed-pore conformation, the polar pore residues are inaccessible. Only the surface hydrophobic residues are exposed. As the pore opens up, inner polar residues become accessible allowing for the binding of hydrophilic bile salts. The pattern of hydrophobic and polar residues within the pore matches the amphipathic patterns within taurocholates, [https://en.wikipedia.org/wiki/Steroid steroids], and [https://en.wikipedia.org/wiki/Thyroid_hormones thyroid hormones]. <Ref name = Qi> Qi X. and Li W. (2022). Unlocking the secrets to human NTCP structure. The Innovation 3(5), 100294. https://doi.org/10.1016/j.xinn.2022.100294 </ref> Using this amphipathic pore, provides the channel with specificity while preventing leakage of other substrates. Essential <scene name='95/952722/Bile_salts_res/1'>bile salt binding residues</scene> form Van der Waals interactions with bile salt substrates, while others form dipole-dipole or ionic interactions. The core domain contributes most of the polar domains, while the panel domain contributes mainly hydrophobic surface.
+A key feature of NTCP is its <scene name='95/952722/Amphipathic_patterns/1'>amphipathic pore</scene> which allows for bile salt transport across the hydrophilic membrane. The pore surface remains {{Template:ColorKey_Hydrophobic}}, while the <scene name='95/952721/Amphipathic_patterns_pore/2'>lining of the open pore</scene> is largely {{Template:ColorKey_Polar}}. In the inward-facing or closed-pore conformation, the polar pore residues are inaccessible. Only the surface hydrophobic residues are exposed. As the pore opens up, inner polar residues become accessible allowing for the binding of hydrophilic bile salts. The pattern of hydrophobic and polar residues within the pore matches the amphipathic patterns within taurocholates, [https://en.wikipedia.org/wiki/Steroid steroids], and [https://en.wikipedia.org/wiki/Thyroid_hormones thyroid hormones]. <Ref name = Qi> Qi X. and Li W. (2022). Unlocking the secrets to human NTCP structure. The Innovation 3(5), 100294. https://doi.org/10.1016/j.xinn.2022.100294 </ref> Using this amphipathic pore, provides the channel with specificity while preventing leakage of other substrates. Essential <scene name='95/952722/Bile_salts_res/1'>bile salt binding residues</scene> form Van der Waals interactions with bile salt substrates, while others form dipole-dipole or ionic interactions. The core domain contributes most of the polar domains, while the panel domain contributes mainly hydrophobic surface.
 === Conformational Change ===