Sandbox GGC14

From Proteopedia

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Acetylcholinesterase

Human acetylcholinesterase (AChE) is an enzyme which inhibits the function acetylcholine by way of a rapid hydrolysis. It is classified as a toxin/ hydrolase and has been linked to things such as snake venom and has been used in the the development of treatment for diseases which involve the nervous system and the transmission of signals to muscles. This specific enzyme has 3 active binding sites and 6 mutations. Each of which either causing a loss of activity or a mis-folding.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Function
2 Disease
3 Relevance
- 3.1 testing
4 Structural highlights

Function

Acetylcholinesterase functions primarily in the synaptic cleft to stop the signal to the neurotransmitter. This is done by way of a rapid hydrolysis reaction of acetylcholine yielding the products acetate, choline and a hydrogen ion. In conjunction with its biological function it has an unusually high catalytic activity because considering the fact that it is a serine hydrolase it functions more closely to the rate of a limitation by diffusion control. [1] A big contributer to the activity of the enzyme is the mutagenesis. The mutations noted are at positions 234, 365, and 478, these are all also the active sites of the enzyme. One happens at the acyl ester intermediate, while the other two are at a sort of charge relay system. The one located in the acyl ester intermediate functions as the main active site. It is located deep in the gorge lined largely by aromatic residues along with many Serines and this specific sites mutation causes a loss in activity.

Another structure that contributes greatly to the function of the protein is the ligand binding and interactions of the molecule. It is important to note that there is a high binding affinity for ligands to the structure. This in turn is what increases the enzymes catalytic rate.

Disease

alzeihmers mutations

Relevance

treatment of diseases

testing

this is noraml

Structural highlights

Scene 1

this is the

Scene 2

this is a view of the

Scene 3

this is a visual of the

Scene 4

This is the veiw of

Scene 5

this is a view of This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

1. Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL. Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target. Structure. 1995 Dec 15;3(12):1355-66. doi: 10.1016/s0969-2126(01)00273-8. PMID: 8747462.

2. Dvir, H., Silman, I., Harel, M., Rosenberry, T. L., & Sussman, J. L. (2010). Acetylcholinesterase: from 3D structure to function. Chemico-biological interactions, 187(1-3), 10–22. https://doi.org/10.1016/j.cbi.2010.01.042

3. Shafferman, A., Kronman, C., Flashner, Y., Leitner, M., Grosfeld, H., Ordentlich, A., Gozes, Y., Cohen, S., Ariel, N., & Barak, D. (1992). Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. The Journal of biological chemistry, 267(25), 17640–17648.

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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 == Function ==
-Acetylcholinesterase functions primarily in the synaptic cleft to stop the signal to the neurotransmitter.  This is done by way of a rapid hydrolysis reaction of acetylcholine yielding the products acetate, choline and a hydrogen ion. In conjunction with its biological function it has an unusually high catalytic activity because considering the fact that it is a serine hydrolase it functions more closely to the rate of a limitation by diffusion control.  [1]  A big contributer to the activity of the enzyme is the presence of its .  The mutations noted are at positions 234, 365, and 478, these are all also the active sites of the enzyme.  One happens at the acyl ester intermediate while the other two are at a sort of charge relay system.
+Acetylcholinesterase functions primarily in the synaptic cleft to stop the signal to the neurotransmitter.  This is done by way of a rapid hydrolysis reaction of acetylcholine yielding the products acetate, choline and a hydrogen ion. In conjunction with its biological function it has an unusually high catalytic activity because considering the fact that it is a serine hydrolase it functions more closely to the rate of a limitation by diffusion control.  [1]  A big contributer to the activity of the enzyme is the mutagenesis.  The mutations noted are at positions 234, 365, and 478, these are all also the active sites of the enzyme.  One happens at the acyl ester intermediate, while the other two are at a sort of charge relay system.  The one located in the acyl ester intermediate functions as the main active site.  It is located deep in the gorge lined largely by aromatic residues along with many Serines and this specific sites mutation causes a loss in activity.
+Another structure that contributes greatly to the function of the protein is the ligand binding and interactions of the molecule. It is important to note that there is a high binding affinity for ligands to the structure.  This in turn is what increases the enzymes catalytic rate.
 == Disease ==