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| - | ==Acetylcholinesterase in complex with tacrine== | ||
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| - | <applet load='1acj' size='300' frame='true' align='right' caption='Insert caption here' /> | ||
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| - | In the crystal structure of Torpedo californica [[acetylcholinesterase]] | ||
| - | (TcAChE) complexed with tacrine (THA), THA's acridine ring is stacked | ||
| - | between the aromatic rings of <scene name='Sandbox_12345/1acj_x/1'>W84 and F330</scene>, near the catalytic triad | ||
| - | of AChE's active site which consists of S200, E327, H440. When | ||
| - | comparing 3 recent complexes of TcAChE, i.e. edrophonium (EDR), | ||
| - | decamethonium (DECA) and THA, the only major conformational difference | ||
| - | between them is seen in the orientation of the phenyl ring of F330. In | ||
| - | the DECA complex it lies parallel to the surface of the gorge; in the | ||
| - | other two complexes it is positioned to make contact with the bound | ||
| - | ligand. This close interaction was confirmed <ref>PMID:8415649</ref> by photoaffinity labeling | ||
| - | by a 3H-labeled photosensitive probe, which labeled, predominantly, | ||
| - | F330 within the active site. Labeling of W279 was also observed. One | ||
| - | mole of label is incorporated per mole of AChE inactivated, indicating | ||
| - | that labeling of W279 and that of F330 are mutually exclusive. The | ||
| - | structural and chemical data, together, show the important role of | ||
| - | aromatic groups as binding sites for quaternary ligands, and they | ||
| - | provide complementary evidence assigning W84 and F330 to the "anionic" | ||
| - | subsite of the active site and W279 to the "peripheral" anionic site. | ||
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| - | <quiz display=simple> | ||
| - | { | ||
| - | |type="{}"} | ||
| - | Name a famous Greek philosopher. | ||
| - | { Aristotle|Plato } | ||
| - | |||
| - | {Question | ||
| - | |type="[]"} | ||
| - | + Correct answer. | ||
| - | - Incorrect answer. | ||
| - | + Correct answer. | ||
| - | - Incorrect answer. | ||
| - | </quiz> | ||
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| - | |||
| - | <references/> | ||
