Sandbox Reserved 969: Difference between revisions
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==3E83: NaK channel== | =='''3E83: NaK channel'''== | ||
<StructureSection load='3e83' size='350' align='right' caption='Cartoon model of the NaK Channel: {{Template:ColorKey_N2CRainbow}}' scene='56/568023/3e83_cartoon_rainbow/4' /> | <StructureSection load='3e83' size='350' align='right' caption='Cartoon model of the NaK Channel: {{Template:ColorKey_N2CRainbow}}' scene='56/568023/3e83_cartoon_rainbow/4' /> | ||
==Introduction== | =='''Introduction'''== | ||
Ion channels are '''transmembrane proteins''' which allow ions to pass through biological membranes. | Ion channels are '''transmembrane proteins''' which allow ions to pass through biological membranes. | ||
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== Structure == | == '''Structure''' == | ||
===General Description=== | ===General Description=== | ||
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Channel opening is a conserved mechanism.The inner helix twist and bend thanks to a conserved glycine residue which is considered as the gating hinge. After this bending, the inner helices twist of 45° around their helical helix and the outer helix tilt tangentially in the same direction by 11° without any twisting motion. As all of helix twist or move inside of a subunit, intra-subunit interactions between inner and outer helix don’t differ a lot. On the contrary, inter-subunit interactions between neighboring inner helix change. In fact, Phe92 swings away and points its side chain towards the central ion conduction pathway due to inner helix bending and the hydrophobic patch slides along the neighboring inner helix by two helical turns and forms new Van der Waals contacts with Phe85. This resulted in a disruption of the bundle crossing and so intra- and inter- subunits interactions in the open state become less important than in the close state. <ref>PMID: 19098917</ref> | Channel opening is a conserved mechanism.The inner helix twist and bend thanks to a conserved glycine residue which is considered as the gating hinge. After this bending, the inner helices twist of 45° around their helical helix and the outer helix tilt tangentially in the same direction by 11° without any twisting motion. As all of helix twist or move inside of a subunit, intra-subunit interactions between inner and outer helix don’t differ a lot. On the contrary, inter-subunit interactions between neighboring inner helix change. In fact, Phe92 swings away and points its side chain towards the central ion conduction pathway due to inner helix bending and the hydrophobic patch slides along the neighboring inner helix by two helical turns and forms new Van der Waals contacts with Phe85. This resulted in a disruption of the bundle crossing and so intra- and inter- subunits interactions in the open state become less important than in the close state. <ref>PMID: 19098917</ref> | ||
== Active Site & Ions | == '''Active Site & Ions Passage''' == | ||
There are '''4 ions binding sites''' in the NaK channel <ref> PMID: 16467789</ref>. This diversity allows by different mechanisms to conduit several cations. They have similar chemical environments but they have '''different ion selectivity'''. Two of them (sites S3 and S4) are conserved, that is to say they are the same than in the high selective K+ channel while S1 and S2 become a vestibular structure where K+ and Na+ ions can diffuse<ref> PMID: 19098915 </ref> .[[Image:biding_sites.jpg|center|00px|The different ions binding site]] | There are '''4 ions binding sites''' in the NaK channel <ref> PMID: 16467789</ref>. This diversity allows by different mechanisms to conduit several cations. They have similar chemical environments but they have '''different ion selectivity'''. Two of them (sites S3 and S4) are conserved, that is to say they are the same than in the high selective K+ channel while S1 and S2 become a vestibular structure where K+ and Na+ ions can diffuse<ref> PMID: 19098915 </ref> .[[Image:biding_sites.jpg|center|00px|The different ions binding site]] | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
== References == | == '''References''' == | ||
<references/> | <references/> | ||
==Contributors== | == '''Contributors''' == | ||
Camille Noblet & Lola Welsch | Camille Noblet & Lola Welsch | ||
