Sandbox GGC14
From Proteopedia
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==Acetylcholinesterase== | ==Acetylcholinesterase== | ||
| + | Human acetylcholinesterase (ACHE) is an enzyme which inhibits the function acetylcholine by way of a rapid hydrolysis. It is classified as a toxin and has been linked to things such as snake venom and has been used in the the development of treatment for Alzheimer's disease. This specific enzyme has 3 active binding sites and 6 mutations. Each of which either causing a loss of activity or a misfolding. | ||
<StructureSection load='1B41' size='340' side='right' caption='Acetylcholinesterase' scene=''> | <StructureSection load='1B41' size='340' side='right' caption='Acetylcholinesterase' scene=''> | ||
This is a default text for your page. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page. Click above on '''edit this page''' to modify. Be careful with the < and > 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 == | == 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 the neurotransmitter acetylcholine yielding the products acetate, choline and hydrogen ion. | ||
== Disease == | == Disease == | ||
| + | alzeihmers | ||
| + | mutations | ||
== Relevance == | == Relevance == | ||
| + | treatment of diseases | ||
===testing=== | ===testing=== | ||
this is noraml | this is noraml | ||
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</StructureSection> | </StructureSection> | ||
== References == | == 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. | ||
| + | 4. | ||
<references/> | <references/> | ||
Revision as of 14:15, 28 April 2021
Acetylcholinesterase
Human acetylcholinesterase (ACHE) is an enzyme which inhibits the function acetylcholine by way of a rapid hydrolysis. It is classified as a toxin and has been linked to things such as snake venom and has been used in the the development of treatment for Alzheimer's disease. This specific enzyme has 3 active binding sites and 6 mutations. Each of which either causing a loss of activity or a misfolding.
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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. 4.
- ↑ 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
