PDBsum entry 1n5m

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
536 a.a. *
IOD ×10
Waters ×551
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of the mouse acetylcholinesterase-gallamin
Structure: Acetylcholinesterase. Chain: a, b. Fragment: catalytic domain. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: ache. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_variant: lambda-zap, lambda-fix cdna, gen expression_system_cell_line: hek 293. Expression_system_cell: human embryonic kidney cells (hek)
2.20Å     R-factor:   0.198     R-free:   0.213
Authors: Y.Bourne,P.Taylor,Z.Radic,P.Marchot
Key ref:
Y.Bourne et al. (2003). Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J, 22, 1. PubMed id: 12505979 DOI: 10.1093/emboj/cdg005
06-Nov-02     Release date:   04-Feb-03    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P21836  (ACES_MOUSE) -  Acetylcholinesterase
614 a.a.
536 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Acetylcholinesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acetylcholine + H2O = choline + acetate
Bound ligand (Het Group name = NAG)
matches with 41.18% similarity
+ H(2)O
= choline
Bound ligand (Het Group name = CO3)
matches with 60.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   17 terms 
  Biological process     synapse assembly   13 terms 
  Biochemical function     carboxylic ester hydrolase activity     9 terms  


DOI no: 10.1093/emboj/cdg005 EMBO J 22:1 (2003)
PubMed id: 12505979  
Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.
Y.Bourne, P.Taylor, Z.Radić, P.Marchot.
The peripheral anionic site on acetylcholinesterase (AChE), located at the active center gorge entry, encompasses overlapping binding sites for allosteric activators and inhibitors; yet, the molecular mechanisms coupling this site to the active center at the gorge base to modulate catalysis remain unclear. The peripheral site has also been proposed to be involved in heterologous protein associations occurring during synaptogenesis or upon neurodegeneration. A novel crystal form of mouse AChE, combined with spectrophotometric analyses of the crystals, enabled us to solve unique structures of AChE with a free peripheral site, and as three complexes with peripheral site inhibitors: the phenylphenanthridinium ligands, decidium and propidium, and the pyrogallol ligand, gallamine, at 2.20-2.35 A resolution. Comparison with structures of AChE complexes with the peptide fasciculin or with organic bifunctional inhibitors unveils new structural determinants contributing to ligand interactions at the peripheral site, and permits a detailed topographic delineation of this site. Hence, these structures provide templates for designing compounds directed to the enzyme surface that modulate specific surface interactions controlling catalytic activity and non-catalytic heterologous protein associations.
  Selected figure(s)  
Figure 1.
Figure 1 PAS ligands (AChE inhibitors) used in this study. Schematic drawings (from top to bottom) of the phenylphenanthridinium ligands propidium (PI; 3,8-diamino-5[3'-(diethylmethylammonio) propyl]-6-phenyl phenanthridinium) and decidium (DI; 3,8-diamino-5[10'- (trimethyl-ammonio) decyl]-6-phenyl phenanthridinium), and of the pyrogallol ligand gallamine (GAL; 2,2',2"-[1,2,3-benzene-triyltris(oxy)]tris[N,N,N-triethylethanamonium]). PI and DI were diiodide salts and GAL was a triiodide.
Figure 5.
Figure 5 Structural comparisons of the DI -mAChE complex with the Fas2 -mAChE complex and the crystalline mAChE tetramer. (A) Close-up view of a superimposition of the DI molecule (orange bonds, blue nitrogen and red oxygen atoms) in the DI -mAChE complex with the interacting central loop (loop II) of Fas2 (yellow) bound to mAChE in the Fas2 -mAChE complex (1KU6), according to all C[ ]atoms of mAChE in the two structures. The Fas2 side chains that match the structural determinants of the DI molecule are displayed as green bonds. (B) Superimposition of the DI molecule (colored as in A) in the DI -mAChE complex with the PAS-occluding short loop (yellow) of subunit A in the mAChE tetrameric assembly (1MAA), according to all C[ ]atoms of mAChE in the DI -mAChE complex and in the tetramer subunit C. Those of the mAChE short loop side chains that match the structural determinants of the DI molecule are displayed as orange bonds. The mAChE molecular surfaces buried at the Fas2 -mAChE complex interface (A) and at the loop -PAS interface (B) are shown in transparency.
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2003, 22, 1-0) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21397996 F.Belluti, M.Bartolini, G.Bottegoni, A.Bisi, A.Cavalli, V.Andrisano, and A.Rampa (2011).
Benzophenone-based derivatives: a novel series of potent and selective dual inhibitors of acetylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation.
  Eur J Med Chem, 46, 1682-1693.  
21064131 M.Amitay, and A.Shurki (2011).
Hydrolysis of organophosphate compounds by mutant butyrylcholinesterase: a story of two histidines.
  Proteins, 79, 352-364.  
20140002 M.K.Kesharwani, B.Ganguly, A.Das, and T.Bandyopadhyay (2010).
Differential binding of bispyridinium oxime drugs with acetylcholinesterase.
  Acta Pharmacol Sin, 31, 313-328.  
20090844 M.S.García-Ayllón, I.Riba-Llena, C.Serra-Basante, J.Alom, R.Boopathy, and J.Sáez-Valero (2010).
Altered levels of acetylcholinesterase in Alzheimer plasma.
  PLoS One, 5, e8701.  
20565748 S.Bremm, T.Schreck, P.Boba, S.Held, and K.Hamacher (2010).
Computing and visually analyzing mutual information in molecular co-evolution.
  BMC Bioinformatics, 11, 330.  
20081206 S.H.Kim, M.Spensley, S.K.Choi, C.P.Calixto, A.F.Pendle, O.Koroleva, P.J.Shaw, and J.W.Brown (2010).
Plant U13 orthologues and orphan snoRNAs identified by RNomics of RNA from Arabidopsis nucleoli.
  Nucleic Acids Res, 38, 3054-3067.  
19225621 E.Meggers (2009).
Targeting proteins with metal complexes.
  Chem Commun (Camb), (), 1001-1010.  
19536291 F.Ekström, A.Hörnberg, E.Artursson, L.G.Hammarström, G.Schneider, and Y.P.Pang (2009).
Structure of HI-6*sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: reactivator mechanism and design.
  PLoS One, 4, e5957.
PDB codes: 2whp 2whq 2whr
19699221 J.Shenouda, P.Green, and L.Sultatos (2009).
An evaluation of the inhibition of human butyrylcholinesterase and acetylcholinesterase by the organophosphate chlorpyrifos oxon.
  Toxicol Appl Pharmacol, 241, 135-142.  
19285445 K.T.Tycowski, M.D.Shu, A.Kukoyi, and J.A.Steitz (2009).
A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles.
  Mol Cell, 34, 47-57.  
19452557 M.Amitay, and A.Shurki (2009).
The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger.
  Proteins, 77, 370-377.  
19292875 M.F.Montenegro, M.T.Moral-Naranjo, E.Muñoz-Delgado, F.J.Campoy, and C.J.Vidal (2009).
Hydrolysis of acetylthiocoline, o-nitroacetanilide and o-nitrotrifluoroacetanilide by fetal bovine serum acetylcholinesterase.
  FEBS J, 276, 2074-2083.  
19292865 M.Pietsch, L.Christian, T.Inhester, S.Petzold, and M.Gütschow (2009).
Kinetics of inhibition of acetylcholinesterase in the presence of acetonitrile.
  FEBS J, 276, 2292-2307.  
19956664 R.Pattanayek, T.Mori, Y.Xu, S.Pattanayek, C.H.Johnson, and M.Egli (2009).
Structures of KaiC circadian clock mutant proteins: a new phosphorylation site at T426 and mechanisms of kinase, ATPase and phosphatase.
  PLoS One, 4, e7529.
PDB codes: 3jzm 3k09 3k0a 3k0c 3k0e 3k0f
19452616 T.A.Slotkin, I.T.Ryde, N.Wrench, J.A.Card, and F.J.Seidler (2009).
Nonenzymatic role of acetylcholinesterase in neuritic sprouting: regional changes in acetylcholinesterase and choline acetyltransferase after neonatal 6-hydroxydopamine lesions.
  Neurotoxicol Teratol, 31, 183-186.  
19109006 T.Hansmann, B.Sanson, J.Stojan, M.Weik, J.L.Marty, and D.Fournier (2009).
Kinetic insight into the mechanism of cholinesterasterase inhibition by aflatoxin B1 to develop biosensors.
  Biosens Bioelectron, 24, 2119-2124.  
19714254 Y.P.Pang, F.Ekström, G.A.Polsinelli, Y.Gao, S.Rana, D.H.Hua, B.Andersson, P.O.Andersson, L.Peng, S.K.Singh, R.K.Mishra, K.Y.Zhu, A.M.Fallon, D.W.Ragsdale, and S.Brimijoin (2009).
Selective and irreversible inhibitors of mosquito acetylcholinesterases for controlling malaria and other mosquito-borne diseases.
  PLoS One, 4, e6851.
PDB code: 2wls
18468882 C.Teller, J.Halámek, J.Zeravík, W.F.Stöcklein, and F.W.Scheller (2008).
Development of a bifunctional sensor using haptenized acetylcholinesterase and application for the detection of cocaine and organophosphates.
  Biosens Bioelectron, 24, 111-117.  
  18226242 C.Vardabasso, L.Manganaro, M.Lusic, A.Marcello, and M.Giacca (2008).
The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds HIV-1 Tat and promotes viral transcription.
  Retrovirology, 5, 8.  
18299393 M.X.Silveyra, G.Evin, M.F.Montenegro, C.J.Vidal, S.Martínez, J.G.Culvenor, and J.Sáez-Valero (2008).
Presenilin 1 interacts with acetylcholinesterase and alters its enzymatic activity and glycosylation.
  Mol Cell Biol, 28, 2908-2919.  
18497745 R.Pattanayek, D.R.Williams, S.Pattanayek, T.Mori, C.H.Johnson, P.L.Stewart, and M.Egli (2008).
Structural model of the circadian clock KaiB-KaiC complex and mechanism for modulation of KaiC phosphorylation.
  EMBO J, 27, 1767-1778.
PDB code: 2qke
18606998 S.K.Cha, B.Ortega, H.Kurosu, K.P.Rosenblatt, M.Kuro-O, and C.L.Huang (2008).
Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1.
  Proc Natl Acad Sci U S A, 105, 9805-9810.  
18636091 Y.Yao, C.B.Harrison, P.L.Freddolino, K.Schulten, and M.L.Mayer (2008).
Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors.
  EMBO J, 27, 2158-2170.
PDB codes: 2rc7 2rc8 2rc9 2rca 2rcb
18093522 D.Araç, A.A.Boucard, E.Ozkan, P.Strop, E.Newell, T.C.Südhof, and A.T.Brunger (2007).
Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions.
  Neuron, 56, 992.
PDB codes: 3biw 3bix
17443135 F.J.Ekström, C.Astot, and Y.P.Pang (2007).
Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes.
  Clin Pharmacol Ther, 82, 282-293.
PDB codes: 2jey 2jez 2jf0
  17565686 G.J.Towers (2007).
The control of viral infection by tripartite motif proteins and cyclophilin A.
  Retrovirology, 4, 40.  
18093521 I.P.Fabrichny, P.Leone, G.Sulzenbacher, D.Comoletti, M.T.Miller, P.Taylor, Y.Bourne, and P.Marchot (2007).
Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion.
  Neuron, 56, 979-991.
PDB codes: 2vh8 2wqz 3be8
17326766 M.S.García-Ayllón, M.X.Silveyra, N.Andreasen, S.Brimijoin, K.Blennow, and J.Sáez-Valero (2007).
Cerebrospinal fluid acetylcholinesterase changes after treatment with donepezil in patients with Alzheimer's disease.
  J Neurochem, 101, 1701-1711.  
  17366821 R.R.Jameson, F.J.Seidler, and T.A.Slotkin (2007).
Nonenzymatic functions of acetylcholinesterase splice variants in the developmental neurotoxicity of organophosphates: chlorpyrifos, chlorpyrifos oxon, and diazinon.
  Environ Health Perspect, 115, 65-70.  
17609268 T.Schaller, L.M.Ylinen, B.L.Webb, S.Singh, and G.J.Towers (2007).
Fusion of cyclophilin A to Fv1 enables cyclosporine-sensitive restriction of human and feline immunodeficiency viruses.
  J Virol, 81, 10055-10063.  
17307283 Y.Cheng, J.K.Suen, Z.Radić, S.D.Bond, M.J.Holst, and J.A.McCammon (2007).
Continuum simulations of acetylcholine diffusion with reaction-determined boundaries in neuromuscular junction models.
  Biophys Chem, 127, 129-139.  
16434405 A.De Jaco, D.Comoletti, Z.Kovarik, G.Gaietta, Z.Radic, O.Lockridge, M.H.Ellisman, and P.Taylor (2006).
A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha,beta-hydrolase fold protein family.
  J Biol Chem, 281, 9667-9676.  
16342323 D.Rochu, C.Cléry-Barraud, F.Renault, A.Chevalier, C.Bon, and P.Masson (2006).
Capillary electrophoresis versus differential scanning calorimetry for the analysis of free enzyme versus enzyme-ligand complexes: in the search of the ligand-free status of cholinesterases.
  Electrophoresis, 27, 442-451.  
17021015 J.M.Bui, and J.A.McCammon (2006).
Protein complex formation by acetylcholinesterase and the neurotoxin fasciculin-2 appears to involve an induced-fit mechanism.
  Proc Natl Acad Sci U S A, 103, 15451-15456.  
16763558 J.P.Colletier, D.Fournier, H.M.Greenblatt, J.Stojan, J.L.Sussman, G.Zaccai, I.Silman, and M.Weik (2006).
Structural insights into substrate traffic and inhibition in acetylcholinesterase.
  EMBO J, 25, 2746-2756.
PDB codes: 2c4h 2c58 2c5f 2c5g
16840314 L.M.Ylinen, Z.Keckesova, B.L.Webb, R.J.Gifford, T.P.Smith, and G.J.Towers (2006).
Isolation of an active Lv1 gene from cattle indicates that tripartite motif protein-mediated innate immunity to retroviral infection is widespread among mammals.
  J Virol, 80, 7332-7338.  
16554805 M.L.Mayer (2006).
Glutamate receptors at atomic resolution.
  Nature, 440, 456-462.  
16794924 P.J.Atzberger, and C.S.Peskin (2006).
A Brownian Dynamics model of kinesin in three dimensions incorporating the force-extension profile of the coiled-coil cargo tether.
  Bull Math Biol, 68, 131-160.  
16751247 R.H.Meltzer, E.Thompson, K.V.Soman, X.Z.Song, J.O.Ebalunode, T.G.Wensel, J.M.Briggs, and S.E.Pedersen (2006).
Electrostatic steering at acetylcholine binding sites.
  Biophys J, 91, 1302-1314.  
16628225 R.Pattanayek, D.R.Williams, S.Pattanayek, Y.Xu, T.Mori, C.H.Johnson, P.L.Stewart, and M.Egli (2006).
Analysis of KaiA-KaiC protein interactions in the cyano-bacterial circadian clock using hybrid structural methods.
  EMBO J, 25, 2017-2028.
PDB code: 2gbl
16619028 S.Cursi, A.Rufini, V.Stagni, I.Condò, V.Matafora, A.Bachi, A.P.Bonifazi, L.Coppola, G.Superti-Furga, R.Testi, and D.Barilà (2006).
Src kinase phosphorylates Caspase-8 on Tyr380: a novel mechanism of apoptosis suppression.
  EMBO J, 25, 1895-1905.  
16837465 Y.Bourne, Z.Radic, G.Sulzenbacher, E.Kim, P.Taylor, and P.Marchot (2006).
Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding.
  J Biol Chem, 281, 29256-29267.
PDB codes: 2h9y 2ha0 2ha2 2ha3 2ha4 2ha5 2ha6 2ha7
17183688 Y.P.Pang (2006).
Novel acetylcholinesterase target site for malaria mosquito control.
  PLoS ONE, 1, e58.  
16641261 Z.Keckesova, L.M.Ylinen, and G.J.Towers (2006).
Cyclophilin A renders human immunodeficiency virus type 1 sensitive to Old World monkey but not human TRIM5 alpha antiviral activity.
  J Virol, 80, 4683-4690.  
15994894 A.S.Ramos, and S.Techert (2005).
Influence of the water structure on the acetylcholinesterase efficiency.
  Biophys J, 89, 1990-2003.  
16121193 B.I.Yeh, Y.K.Kim, W.Jabbar, and C.L.Huang (2005).
Conformational changes of pore helix coupled to gating of TRPV5 by protons.
  EMBO J, 24, 3224-3234.  
15685212 L.E.Kennard, J.R.Chumbley, K.M.Ranatunga, S.J.Armstrong, E.L.Veale, and A.Mathie (2005).
Inhibition of the human two-pore domain potassium channel, TREK-1, by fluoxetine and its metabolite norfluoxetine.
  Br J Pharmacol, 144, 821-829.  
16140735 L.M.Ylinen, Z.Keckesova, S.J.Wilson, S.Ranasinghe, and G.J.Towers (2005).
Differential restriction of human immunodeficiency virus type 2 and simian immunodeficiency virus SIVmac by TRIM5alpha alleles.
  J Virol, 79, 11580-11587.  
15964270 T.Roenneberg, and M.Merrow (2005).
Circadian clocks: translation.
  Curr Biol, 15, R470-R473.  
15221019 C.H.Johnson, and M.Egli (2004).
Visualizing a biological clockwork's cogs.
  Nat Struct Mol Biol, 11, 584-585.  
15175651 C.Heurteaux, N.Guy, C.Laigle, N.Blondeau, F.Duprat, M.Mazzuca, L.Lang-Lazdunski, C.Widmann, M.Zanzouri, G.Romey, and M.Lazdunski (2004).
TREK-1, a K+ channel involved in neuroprotection and general anesthesia.
  EMBO J, 23, 2684-2695.  
15345562 E.D.Moore, T.Voigt, Y.M.Kobayashi, G.Isenberg, F.S.Fay, M.F.Gallitelli, and C.Franzini-Armstrong (2004).
Organization of Ca2+ release units in excitable smooth muscle of the guinea-pig urinary bladder.
  Biophys J, 87, 1836-1847.  
14744870 J.Botos, W.Xian, D.F.Smith, and C.L.Smith (2004).
Progesterone receptor deficient in chromatin binding has an altered cellular state.
  J Biol Chem, 279, 15231-15239.  
15236332 J.Zeng, A.J.Hassan, and C.R.Morales (2004).
Study of the mouse sortilin gene: Effects of its transient silencing by RNA interference in TM4 Sertoli cells.
  Mol Reprod Dev, 68, 469-475.  
15454528 L.Dickson, S.Connell, H.R.Huang, R.M.Henke, L.Liu, and P.S.Perlman (2004).
Abortive transposition by a group II intron in yeast mitochondria.
  Genetics, 168, 77-87.  
14766177 M.S.Horning, and M.L.Mayer (2004).
Regulation of AMPA receptor gating by ligand binding core dimers.
  Neuron, 41, 379-388.  
14996813 S.R.Casjens, E.B.Gilcrease, W.M.Huang, K.L.Bunny, M.L.Pedulla, M.E.Ford, J.M.Houtz, G.F.Hatfull, and R.W.Hendrix (2004).
The pKO2 linear plasmid prophage of Klebsiella oxytoca.
  J Bacteriol, 186, 1818-1832.  
14757816 Y.Bourne, H.C.Kolb, Z.Radić, K.B.Sharpless, P.Taylor, and P.Marchot (2004).
Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
  Proc Natl Acad Sci U S A, 101, 1449-1454.
PDB codes: 1q83 1q84
15479823 Y.Ikeda, L.M.Ylinen, M.Kahar-Bador, and G.J.Towers (2004).
Influence of gag on human immunodeficiency virus type 1 species-specific tropism.
  J Virol, 78, 11816-11822.  
15347809 Y.Xu, T.Mori, R.Pattanayek, S.Pattanayek, M.Egli, and C.H.Johnson (2004).
Identification of key phosphorylation sites in the circadian clock protein KaiC by crystallographic and mutagenetic analyses.
  Proc Natl Acad Sci U S A, 101, 13933-13938.
PDB code: 1u9i
15215191 Z.J.Lan, X.Xu, and A.J.Cooney (2004).
Differential oocyte-specific expression of Cre recombinase activity in GDF-9-iCre, Zp3cre, and Msx2Cre transgenic mice.
  Biol Reprod, 71, 1469-1474.  
15249687 Z.Keckesova, L.M.Ylinen, and G.J.Towers (2004).
The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities.
  Proc Natl Acad Sci U S A, 101, 10780-10785.  
14525991 B.I.Yeh, T.J.Sun, J.Z.Lee, H.H.Chen, and C.L.Huang (2003).
Mechanism and molecular determinant for regulation of rabbit transient receptor potential type 5 (TRPV5) channel by extracellular pH.
  J Biol Chem, 278, 51044-51052.  
14645596 C.Besnier, L.Ylinen, B.Strange, A.Lister, Y.Takeuchi, S.P.Goff, and G.J.Towers (2003).
Characterization of murine leukemia virus restriction in mammals.
  J Virol, 77, 13403-13406.  
14678739 H.C.Kolb, and K.B.Sharpless (2003).
The growing impact of click chemistry on drug discovery.
  Drug Discov Today, 8, 1128-1137.  
12851386 J.L.Johnson, B.Cusack, T.F.Hughes, E.H.McCullough, A.Fauq, P.Romanovskis, A.F.Spatola, and T.L.Rosenberry (2003).
Inhibitors tethered near the acetylcholinesterase active site serve as molecular rulers of the peripheral and acylation sites.
  J Biol Chem, 278, 38948-38955.  
14517262 L.Ripaud, L.Maillet, and C.Cullin (2003).
The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products.
  EMBO J, 22, 5251-5259.  
12702719 M.Gallardo, R.Luna, H.Erdjument-Bromage, P.Tempst, and A.Aguilera (2003).
Nab2p and the Thp1p-Sac3p complex functionally interact at the interface between transcription and mRNA metabolism.
  J Biol Chem, 278, 24225-24232.  
12768202 M.Springer, and C.Portier (2003).
More than one way to skin a cat: translational autoregulation by ribosomal protein S15.
  Nat Struct Biol, 10, 420-422.  
14576316 R.Onclercq-Delic, P.Calsou, C.Delteil, B.Salles, D.Papadopoulo, and M.Amor-Guéret (2003).
Possible anti-recombinogenic role of Bloom's syndrome helicase in double-strand break processing.
  Nucleic Acids Res, 31, 6272-6282.  
15035023 S.S.Golden, and S.R.Canales (2003).
Cyanobacterial circadian clocks--timing is everything.
  Nat Rev Microbiol, 1, 191-199.  
12869558 Y.Nicolet, O.Lockridge, P.Masson, J.C.Fontecilla-Camps, and F.Nachon (2003).
Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
  J Biol Chem, 278, 41141-41147.
PDB codes: 1p0i 1p0m 1p0p 1p0q
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.