1ax9 › Citations

Static Laue diffraction studies on acetylcholinesterase.

Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL
Acta Crystallogr D Biol Crystallogr 54 1359-66 (1998)
Related entries: 1acj, 1acl, 2ack

Cited: 22 times
EuropePMC logo PMID: 10089512

Abstract

Acetylcholinesterase (AChE) is one of nature's fastest enzymes, despite the fact that its three-dimensional structure reveals its active site to be deeply sequestered within the molecule. This raises questions with respect to traffic of substrate to, and products from, the active site, which may be investigated by time-resolved crystallography. In order to address one aspect of the feasibility of performing time-resolved studies on AChE, a data set has been collected using the Laue technique on a trigonal crystal of Torpedo californica AChE soaked with the reversible inhibitor edrophonium, using a total X-ray exposure time of 24 ms. Electron-density maps obtained from the Laue data, which are of surprisingly good quality compared with similar maps from monochromatic data, show essentially the same features. They clearly reveal the bound ligand, as well as a structural change in the conformation of the active-site Ser200 induced upon binding.

Reviews - 1ax9 mentioned but not cited (1)

  1. Molecular dynamics simulations: advances and applications. Hospital A, Goñi JR, Orozco M, Gelpí JL. Adv Appl Bioinform Chem 8 37-47 (2015)

Articles - 1ax9 mentioned but not cited (5)

  1. Structure-based search for new inhibitors of cholinesterases. Bajda M, Więckowska A, Hebda M, Guzior N, Sotriffer CA, Malawska B. Int J Mol Sci 14 5608-5632 (2013)
  2. Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics. Xu Y, Colletier JP, Weik M, Jiang H, Moult J, Silman I, Sussman JL. Biophys J 95 2500-2511 (2008)
  3. Pharmacophore-based virtual screening versus docking-based virtual screening: a benchmark comparison against eight targets. Chen Z, Li HL, Zhang QJ, Bao XG, Yu KQ, Luo XM, Zhu WL, Jiang HL. Acta Pharmacol Sin 30 1694-1708 (2009)
  4. A novel interaction fingerprint derived from per atom score contributions: exhaustive evaluation of interaction fingerprint performance in docking based virtual screening. Jasper JB, Humbeck L, Brinkjost T, Koch O. J Cheminform 10 15 (2018)
  5. Exploring different virtual screening strategies for acetylcholinesterase inhibitors. Mishra N, Basu A. Biomed Res Int 2013 236850 (2013)


Reviews citing this publication (1)

  1. Molecular interactions of cholinesterases inhibitors using in silico methods: current status and future prospects. Khan MT. N Biotechnol 25 331-346 (2009)

Articles citing this publication (15)

  1. Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock. Bikadi Z, Hazai E. J Cheminform 1 15 (2009)
  2. Specific chemical and structural damage to proteins produced by synchrotron radiation. Weik M, Ravelli RB, Kryger G, McSweeney S, Raves ML, Harel M, Gros P, Silman I, Kroon J, Sussman JL. Proc Natl Acad Sci U S A 97 623-628 (2000)
  3. Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica. Koellner G, Kryger G, Millard CB, Silman I, Sussman JL, Steiner T. J Mol Biol 296 713-735 (2000)
  4. Interactions in native binding sites cause a large change in protein dynamics. Ming D, Wall ME. J Mol Biol 358 213-223 (2006)
  5. Interaction kinetics of reversible inhibitors and substrates with acetylcholinesterase and its fasciculin 2 complex. Radić Z, Taylor P. J Biol Chem 276 4622-4633 (2001)
  6. The consequences of scoring docked ligand conformations using free energy correlations. Spyrakis F, Amadasi A, Fornabaio M, Abraham DJ, Mozzarelli A, Kellogg GE, Cozzini P. Eur J Med Chem 42 921-933 (2007)
  7. Design and activity of cationic fullerene derivatives as inhibitors of acetylcholinesterase. Pastorin G, Marchesan S, Hoebeke J, Da Ros T, Ehret-Sabatier L, Briand JP, Prato M, Bianco A. Org Biomol Chem 4 2556-2562 (2006)
  8. Molecular docking and receptor-specific 3D-QSAR studies of acetylcholinesterase inhibitors. Deb PK, Sharma A, Piplani P, Akkinepally RR. Mol Divers 16 803-823 (2012)
  9. Molecular docking and 3D-QSAR studies of 2-substituted 1-indanone derivatives as acetylcholinesterase inhibitors. Shen LL, Liu GX, Tang Y. Acta Pharmacol Sin 28 2053-2063 (2007)
  10. Docking of the alkaloid geissospermine into acetylcholinesterase: a natural scaffold targeting the treatment of Alzheimer's disease. Araújo JQ, Lima JA, Pinto Ada C, de Alencastro RB, Albuquerque MG. J Mol Model 17 1401-1412 (2011)
  11. Drug-like leads for steric discrimination between substrate and inhibitors of human acetylcholinesterase. Wildman SA, Zheng X, Sept D, Auletta JT, Rosenberry TL, Marshall GR. Chem Biol Drug Des 78 495-504 (2011)
  12. Nanosecond dynamics of acetylcholinesterase near the active center gorge. Boyd AE, Dunlop CS, Wong L, Radic Z, Taylor P, Johnson DA. J Biol Chem 279 26612-26618 (2004)
  13. Investigation of the binding mode of (-)-meptazinol and bis-meptazinol derivatives on acetylcholinesterase using a molecular docking method. Xie Q, Tang Y, Li W, Wang XH, Qiu ZB. J Mol Model 12 390-397 (2006)
  14. An analysis of acetylcholinesterase sequence for predicting mechanisms of its non-catalytic actions. Srivatsan M. Bioinformation 1 281-284 (2006)
  15. Synthesis, kinetic studies and molecular modeling of novel tacrine dimers as cholinesterase inhibitors. de Aquino RA, Modolo LV, Alves RB, de Fátima Â. Org Biomol Chem 11 8395-8409 (2013)


Related citations provided by authors (3)

  1. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.. Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL Proc Natl Acad Sci U S A 90 9031-5 (1993)
  2. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I Science 253 872-9 (1991)
  3. Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C.. Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I J Mol Biol 203 821-3 (1988)

Quick links