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. 1997 Jan 1;25(1):143–146. doi: 10.1093/nar/25.1.143

The alpha/beta fold family of proteins database and the cholinesterase gene server ESTHER.

X Cousin 1, T Hotelier 1, K Giles 1, P Lievin 1, J P Toutant 1, A Chatonnet 1
PMCID: PMC146416  PMID: 9016525

Abstract

ESTHER (for esterases, alpha/betahydrolase enzyme and relatives) is a database of sequences phylogenetically related to cholinesterases. These sequences define a homogeneous group of enzymes (carboxylesterases, lipases and hormone-sensitive lipases) sharing a similar structure of a central beta-sheet surrounded by alpha-helices. Among these proteins a wide range of functions can be found (hydrolases, adhesion molecules, hormone precursors). The purpose of ESTHER is to help comparison of structures and functions of members of the family. Since the last release, new features have been added to the server. A BLAST comparison tool allows sequence homology searches within the database sequences. New sections are available: kinetics and inhibitors of cholinesterases, fasciculin-acetylcholinesterase interaction and a gene structure review. The mutation analysis compilation has been improved with three-dimensional images. A mailing list has been created.

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Selected References

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  1. Abramson S. N., Radic Z., Manker D., Faulkner D. J., Taylor P. Onchidal: a naturally occurring irreversible inhibitor of acetylcholinesterase with a novel mechanism of action. Mol Pharmacol. 1989 Sep;36(3):349–354. [PubMed] [Google Scholar]
  2. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  3. Ashani Y., Grunwald J., Kronman C., Velan B., Shafferman A. Role of tyrosine 337 in the binding of huperzine A to the active site of human acetylcholinesterase. Mol Pharmacol. 1994 Mar;45(3):555–560. [PubMed] [Google Scholar]
  4. Bourne Y., Taylor P., Marchot P. Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell. 1995 Nov 3;83(3):503–512. doi: 10.1016/0092-8674(95)90128-0. [DOI] [PubMed] [Google Scholar]
  5. Cousin X., Hotelier T., Liévin P., Toutant J. P., Chatonnet A. A cholinesterase genes server (ESTHER): a database of cholinesterase-related sequences for multiple alignments, phylogenetic relationships, mutations and structural data retrieval. Nucleic Acids Res. 1996 Jan 1;24(1):132–136. doi: 10.1093/nar/24.1.132. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Harel M., Kleywegt G. J., Ravelli R. B., Silman I., Sussman J. L. 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):1355–1366. doi: 10.1016/s0969-2126(01)00273-8. [DOI] [PubMed] [Google Scholar]
  7. Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M., Hirth C., Axelsen P. H., Silman I., Sussman J. L. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc Natl Acad Sci U S A. 1993 Oct 1;90(19):9031–9035. doi: 10.1073/pnas.90.19.9031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hein J. Unified approach to alignment and phylogenies. Methods Enzymol. 1990;183:626–645. doi: 10.1016/0076-6879(90)83041-7. [DOI] [PubMed] [Google Scholar]
  9. Karlsson E., Mbugua P. M., Rodriguez-Ithurralde D. Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps. J Physiol (Paris) 1984;79(4):232–240. [PubMed] [Google Scholar]
  10. Krejci E., Duval N., Chatonnet A., Vincens P., Massoulié J. Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6647–6651. doi: 10.1073/pnas.88.15.6647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lockridge O. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol Ther. 1990;47(1):35–60. doi: 10.1016/0163-7258(90)90044-3. [DOI] [PubMed] [Google Scholar]
  12. Massoulié J., Pezzementi L., Bon S., Krejci E., Vallette F. M. Molecular and cellular biology of cholinesterases. Prog Neurobiol. 1993 Jul;41(1):31–91. doi: 10.1016/0301-0082(93)90040-y. [DOI] [PubMed] [Google Scholar]
  13. Mesulam M. M., Asuncion Morán M. Cholinesterases within neurofibrillary tangles related to age and Alzheimer's disease. Ann Neurol. 1987 Aug;22(2):223–228. doi: 10.1002/ana.410220206. [DOI] [PubMed] [Google Scholar]
  14. Ollis D. L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S. M., Harel M., Remington S. J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992 Apr;5(3):197–211. doi: 10.1093/protein/5.3.197. [DOI] [PubMed] [Google Scholar]
  15. Richardson D. C., Richardson J. S. The kinemage: a tool for scientific communication. Protein Sci. 1992 Jan;1(1):3–9. doi: 10.1002/pro.5560010102. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schrag J. D., Li Y. G., Wu S., Cygler M. Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature. 1991 Jun 27;351(6329):761–764. doi: 10.1038/351761a0. [DOI] [PubMed] [Google Scholar]
  17. Smyth K. A., Russell R. J., Oakeshott J. G. A cluster of at least three esterase genes in Lucilia cuprina includes malathion carboxylesterase and two other esterases implicated in resistance to organophosphates. Biochem Genet. 1994 Dec;32(11-12):437–453. doi: 10.1007/BF00566064. [DOI] [PubMed] [Google Scholar]
  18. Sussman J. L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 1991 Aug 23;253(5022):872–879. doi: 10.1126/science.1678899. [DOI] [PubMed] [Google Scholar]
  19. Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994 Nov 11;22(22):4673–4680. doi: 10.1093/nar/22.22.4673. [DOI] [PMC free article] [PubMed] [Google Scholar]

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