The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II
Abstract
Structures of recombinant wild-type human acetylcholinesterase and of its E202Q mutant as complexes with fasciculin-II, a 'three-finger' polypeptide toxin purified from the venom of the eastern green mamba (Dendroaspis angusticeps), are reported. The structure of the complex of the wild-type enzyme was solved to 2.8 A resolution by molecular replacement starting from the structure of the complex of Torpedo californica acetylcholinesterase with fasciculin-II and verified by starting from a similar complex with mouse acetylcholinesterase. The overall structure is surprisingly similar to that of the T. californica enzyme with fasciculin-II and, as expected, to that of the mouse acetylcholinesterase complex. The structure of the E202Q mutant complex was refined starting from the corresponding wild-type human acetylcholinesterase structure, using the 2.7 A resolution data set collected. Comparison of the two structures shows that removal of the charged group from the protein core and its substitution by a neutral isosteric moiety does not disrupt the functional architecture of the active centre. One of the elements of this architecture is thought to be a hydrogen-bond network including residues Glu202, Glu450, Tyr133 and two bridging molecules of water, which is conserved in other vertebrate acetylcholinesterases as well as in the human enzyme. The present findings are consistent with the notion that the main role of this network is the proper positioning of the Glu202 carboxylate relative to the catalytic triad, thus defining its functional role in the interaction of acetylcholinesterase with substrates and inhibitors.
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Cites
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Self-citationPrimary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence
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Self-citationAcetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
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Structures of Human Acetylcholinesterase in Complex with Pharmacologically Important Ligands
Cheung, J., Rudolph, M. J., Burshteyn, F., Cassidy, M. S., Gary, E. N., Love, J., Franklin, M. C., & Height, J. J. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300871x · Cited by 1,356
Network Analysis of Protein Structures Identifies Functional Residues
Amitai, G., Shemesh, A., Sitbon, E., Shklar, M., Netanely, D., Venger, I., & Pietrokovski, S. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.055 · Cited by 499
Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
Bourne, Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg005 · Cited by 488
Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation
Bourne, Y., Kolb, H. C., Radić, Z., Sharpless, K. B., Taylor, P., & Marchot, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308206100 · Cited by 332
Acetylcholinesterase: How is structure related to function?
Silman, I., & Sussman, J. L. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.05.035 · Cited by 263
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Metadata
- Authors
- Kryger, G., Harel, M., Giles, K., Toker, L., Velan, B., Lazar, A., Kronman, C., Barak, D., Ariel, N., Shafferman, A., Silman, I., & Sussman, J. L.
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 2000-11-01
- Volume
- 56
- Issue
- 11
- Pages
- 1385-1394
- ISSN
- 0907-4449 (ISSN-L)
- OpenAlex
- W2143410390
- Cited by
- 310
- References
- 27
- FWCI
- 6.51
- Type
- journal article
- Language
- en
- Open access
- closed
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