Sandbox GGC14

Acetylcholinesterase

spinqualitylabelsall models Acetylcholinesterase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 or to the article describing Jmol 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 this is noraml Structural highlights Scene 1 this is the acetylcholinesterase protein Scene 2 this is a view of the protein ligand Scene 3 this is a visual of the active binding sites Scene 4 This is the veiw of mutations Scene 5 this is a view of binding pockets This is a sample scene created with SAT to color by Group, and another to make a transparent representation 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.