Sandbox 1eve

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(New page: ==Example page for E2020-TcAChE complex (1eve)== <StructureSection load='1eve' size='340' side='right' caption='GFP (PDB entry 1eve' scene=''> [[Image:1eve.Workshop.gif|thumb|left|350...)
Current revision (14:25, 5 July 2024) (edit) (undo)
 
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==Example page for E2020-TcAChE complex (1eve)==
==Example page for E2020-TcAChE complex (1eve)==
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<StructureSection load='1eve' size='340' side='right' caption='GFP (PDB entry [[1eve]]' scene=''>
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<StructureSection load='1eve' size='340' side='right' caption='PDB entry [[1eve]]' scene='29/2908/1eve_e20_cartoon/3'>
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[[Image:1eve.Workshop.gif|thumb|left|350px|Green fluorescent protein (1eve)]]
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[[Image:1eve.Workshop.jpg|thumb|left|250px|E2020 with active site and interacts]]
== Introduction ==
== Introduction ==
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Green fluorescent protein ('''GFP'''), originally isolated from the jellyfish Aequorea victoria (PDB entry [[1ema]]), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.
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E2020, marketed as Aricept, is a member of a large family of N-benzylpiperidine- based acetylcholinesterase (AChE) inhibitors developed, synthesized and evaluated by the Elsai Company in Japan. These Inhibitors were designed on the basis of QSAR studies, prior to elucidation of the three-dimensional structure of Torpedo californica AChE (TCAChE). It significantly enhances performance in animal models of cholinergic hypofunction and has a high affinity for AChE. binding to both electric eel and mouse AChE in the nanomolar range.
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<scene name='10/1052408/E2020_and_aricept/3'>E2020 and TcAChE</scene>.
== Exploring the Structure ==
== Exploring the Structure ==
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GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The <scene name='10/1052406/Gfp_1ema/5'>chromophore</scene>,responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.<ref>PMID:8703075</ref>
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<scene name='10/1052408/E2020_space_fill/5'>E2020</scene> has a unique orientation along the active-site gorge, extending from the anionic subsite of the active site, at the bottom, to the peripheral anlonic site, at the top, via aromatic stacking interactions with conserved aromatic acid residues. E2020 does not, however, interact directly with either the catalytic triad or the 'oxyanion hole', but only indirectly via solvent molecules.
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<ref>PMID:10368299</ref>
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</StructureSection>
== References ==
== References ==
<references/>
<references/>
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==Quiz==
 
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<quiz display=simple>
 
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{How many alpha helices are in this structure?}
 
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- One
 
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- None
 
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+ Eleven
 
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- Twelve
 
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</Quiz>
 

Current revision

Example page for E2020-TcAChE complex (1eve)

PDB entry 1eve

Drag the structure with the mouse to rotate

References

  1. Kryger G, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs. Structure. 1999 Mar 15;7(3):297-307. PMID:10368299
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