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Sandbox 12005

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(New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...)
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==Your Heading Here (maybe something like 'Structure')==
==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='1acj' size='340' side='right' caption='Acetylcholinesterase with Tacrine bound to it'>
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This is a default text for your page '''Sandbox 12005'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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to the rescue.
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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.
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== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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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.
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1ACJ* shows the crystal structure of Torpedo californica acetylcholinesterase (TcAChE) complexed with tacrine.
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Tacrine was the first cholinesterase inhibitor approved for the treatment of Alzheimer's disease.
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Tacrine’s ringed structure is stacked between the aromatic rings of Trp84 and Phe330<ref>PMID:8415649</ref>.
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 09:27, 19 June 2017

Your Heading Here (maybe something like 'Structure')

Acetylcholinesterase with Tacrine bound to it

Drag the structure with the mouse to rotate

References

  1. ↑ Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc Natl Acad Sci U S A. 1993 Oct 1;90(19):9031-5. PMID:8415649
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