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Sandbox Reserved 1793
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<StructureSection load='' size='350' side='right' scene='95/952721/Structure_overview/4'> | <StructureSection load='' size='350' side='right' scene='95/952721/Structure_overview/4'> | ||
| - | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
[[Image:Slicedsurfaceoverview.png|300px|right|thumb]] | [[Image:Slicedsurfaceoverview.png|300px|right|thumb]] | ||
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== Structure == | == Structure == | ||
| - | <scene name='95/952721/Sodium_binding/2'>two sodium binding sites</scene> | + | NTCP, among others in the SLC10 family, have <scene name='95/952721/Sodium_binding/2'>two sodium binding sites</scene>. Many polar and positively charged residues help hold the sodium ions in place creating strong ionic bonds. The high level of conservation among sodium binding placement and interacting residues suggests sodium binding is coupled to bile salt transport. Additional mutations in the X-motif have shown that bile salt transport function is lost also suggesting that sodium acts as a positive allosteric effector of bile salt binding. |
<scene name='95/952721/Hydrophobic_channel/8'>hydrophilic channel</scene> | <scene name='95/952721/Hydrophobic_channel/8'>hydrophilic channel</scene> | ||
Revision as of 18:21, 28 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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