Sandbox GGC14

AcetylcholinesteraseAcetylcholinesterase

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 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. 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.

spinqualitylabelsall models Acetylcholinesterase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ReferencesReferences

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.