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<Ref name = "Goutam"> Goutam, K., Ielasi, F.S., Pardon, E. et al. Structural basis of sodium-dependent bile salt uptake into the liver. Nature 606, 1015–1020 (2022). [https://doi.org/10.1038/s41586-022-04723-z DOI: 10.1038/s41586-022-04723-z]. </Ref> It is understood that these sodium binding sites facilitate changes from open-pore to closed pore states of NTCP that allow for the binding or release of bile salts. Closed-pore state is favored in the absence of sodium ions, while open-pore state is favored in the presence of sodium ions. This also allows for sodium concentrations to regulate uptake of taurocholates. When intracellular sodium levels are higher, open-pore state is favored allowing for the diffusion of taurocholates. However, when extracellular sodium levels are high, closed-state is favored preventing diffusion of taurocholates. <ref name="Goutam"/> | <Ref name = "Goutam"> Goutam, K., Ielasi, F.S., Pardon, E. et al. Structural basis of sodium-dependent bile salt uptake into the liver. Nature 606, 1015–1020 (2022). [https://doi.org/10.1038/s41586-022-04723-z DOI: 10.1038/s41586-022-04723-z]. </Ref> It is understood that these sodium binding sites facilitate changes from open-pore to closed pore states of NTCP that allow for the binding or release of bile salts. Closed-pore state is favored in the absence of sodium ions, while open-pore state is favored in the presence of sodium ions. This also allows for sodium concentrations to regulate uptake of taurocholates. When intracellular sodium levels are higher, open-pore state is favored allowing for the diffusion of taurocholates. However, when extracellular sodium levels are high, closed-state is favored preventing diffusion of taurocholates. <ref name="Goutam"/> | ||
| - | The <scene name='95/952721/Hydrophobic_channel/8'>amphipathic pore</scene> is also characteristic of NTCP. The pore surface remains {{Template:ColorKey_Hydrophobic}}, while lining of the open pore state is largely {{Template:ColorKey_Polar}}. This pattern is believed to follow similar patterns within taurocholate and other NTCP substrates such as steroids and statins. <ref name="Goutam"/> Thus the channel provides specificity while preventing leakage of other substrates. When observing the relevant <scene name='95/952721/Bile_salts_res/3'>bile salt binding residues</scene> it is shown that some residues form Van der waals interactions while others will form dipole-dipole or ionic interactions with bile salt substrates. The core domain appears to contribute most of the polar domains, while the panel domain contributes more hydrophobic residues. | + | The <scene name='95/952721/Hydrophobic_channel/8'>amphipathic pore</scene> is also characteristic of NTCP. The pore surface remains {{Template:ColorKey_Hydrophobic}}, while lining of the open pore state is largely {{Template:ColorKey_Polar}}. This pattern is believed to follow similar amphipathic patterns within taurocholate and other NTCP substrates, such as steroids and statins. <ref name="Goutam"/> Thus the channel provides specificity while preventing leakage of other substrates. When observing the relevant <scene name='95/952721/Bile_salts_res/3'>bile salt binding residues</scene> it is shown that some residues form Van der waals interactions while others will form dipole-dipole or ionic interactions with bile salt substrates. The core domain appears to contribute most of the polar domains, while the panel domain contributes more hydrophobic residues. |
=== Conformational Change === | === Conformational Change === | ||
Revision as of 01:12, 29 March 2023
| This Sandbox is Reserved from February 27 through August 31, 2023 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1765 through Sandbox Reserved 1795. |
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Sodium Bile Salt Co-Transporting Protein
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References
- ↑ 1.0 1.1 1.2 Goutam, K., Ielasi, F.S., Pardon, E. et al. Structural basis of sodium-dependent bile salt uptake into the liver. Nature 606, 1015–1020 (2022). DOI: 10.1038/s41586-022-04723-z.
