Sandbox Reserved 969: Difference between revisions

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{{Sandbox_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Sandbox_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
==Your Heading Here (maybe something like 'Structure')==
==3E83: NaK channel==
<StructureSection load='3e83' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='3e83' size='350' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; 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.
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.


== Function ==
==Introduction==
Ion channels are '''transmembrane proteins''' which allow ions to pass through biological membranes. Some of these channels are very selective, others have a low level of selectivity. The NaK channel is a '''non-selective''' one : It conduits cations more than anions but it let pass several cations : Na+, K+, Rb+, and Ca2+ [1.1].
Understanding how these channels work is important because in the organism a lot of '''messages''' are transmitted through electric currents (which are '''ionic currents''' across the membrane) : nerves impulse, photoreceptors, etc. Thus, these not very selective NaK channels are very interesting for the inhibition of intercellular messages for instance.


== Disease ==


== Relevance ==
== Structure ==
 
== Active Site & Ions Passing ==
There are '''4 ions binding sites''' in the NaK channel [1]. 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 [2].
[[Image:biding_sites.jpg]]
 
We will see for every binding site how his structure allows the passage of one or several ions.
 
== Regulation ==


== Structural highlights ==
== Structural highlights ==