From Proteopedia
proteopedia linkproteopedia link 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.
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.
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
alzeihmers
mutations
Relevance
treatment of diseases
testing
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Structural highlights
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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.
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- ↑ 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
