Acetylcholinesterase

For other uses, see Ache.

strates and inhibitors. The cationic substrates are not

bound by a negatively-charged amino acid in the anionic
site, but by interaction of 14 aromatic residues that line
the gorge leading to the active site.[6][7][8] All 14 amino
acids in the aromatic gorge are highly conserved across
dierent species.[9] Among the aromatic amino acids,
tryptophan 84 is critical and its substitution with alanine
results in a 3000-fold decrease in reactivity.[10] The gorge
penetrates half way through the enzyme and is approximately 20 angstroms long. The active site is located 4
angstroms from the bottom of the molecule.[11]

Acetylcholinesterase, also known as AChE or

acetylhydrolase, is a hydrolase that hydrolyzes the
neurotransmitter acetylcholine. AChE is found at mainly
neuromuscular junctions and cholinergic brain synapses,
where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It
is the primary target of inhibition by organophosphorus
compounds such as nerve agents and pesticides.

The esteratic subsite, where acetylcholine is hydrolyzed

to acetate and choline, contains the catalytic triad of three
amino acids: serine 200, histidine 440 and glutamate 327.
These three amino acids are similar to the triad in other
serine proteases except that the glutamate is the third
member rather than aspartate. Moreover, the triad is of
opposite chirality to that of other proteases.[12] The hydrolysis reaction of the carboxyl ester leads to the formation of an acyl-enzyme and free choline. Then, the
acyl-enzyme undergoes nucleophilic attack by a water
molecule, assisted by the histidine 440 group, liberating
acetic acid and regenerating the free enzyme.[13][14][15][16]

Enzyme structure and mechanism

2 Biological function
During neurotransmission, ACh is released from the
nerve into the synaptic cleft and binds to ACh receptors
on the post-synaptic membrane, relaying the signal from
the nerve. AChE, also located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing
ACh. The liberated choline is taken up again by the
pre-synaptic nerve and ACh is synthetized by combining with acetyl-CoA through the action of choline acetyltransferase.[17][18][19]
AChe mechanism of action[1]

3 Disease relevance

AChE has a very high catalytic activity - each molecule of

AChE degrades about 25000 molecules of acetylcholine
(ACh) per second, approaching the limit allowed by
diusion of the substrate.[2][3] The active site of AChE
comprises 2 subsites - the anionic site and the esteratic
subsite. The structure and mechanism of action of AChE
have been elucidated from the crystal structure of the
enzyme.[4][5]

Main article: Acetylcholinesterase inhibitor

For a cholinergic neuron to receive another impulse, ACh

must be released from the ACh receptor. This occurs
only when the concentration of ACh in the synaptic cleft
is very low. Inhibition of AChE leads to accumulaThe anionic subsite accommodates the positive quater- tion of ACh in the synaptic cleft and results in impeded
nary amine of acetylcholine as well as other cationic sub- neurotransmission.[20]
1

ACHE GENE

4 Distribution
AChE is found in many types of conducting tissue: nerve
and muscle, central and peripheral tissues, motor and
sensory bers, and cholinergic and noncholinergic bers.
The activity of AChE is higher in motor neurons than in
sensory neurons.[31][32][33]
Acetylcholinesterase is also found on the red blood cell
membranes, where dierent forms constitute the Yt
blood group antigens.[34] Acetylcholinesterase exists in
multiple molecular forms, which possess similar catalytic
properties, but dier in their oligomeric assembly and
mode of attachment to the cell surface.

5 AChE gene

Mechanism of Inhibitors of AChE

Irreversible inhibitors of AChE may lead to muscular paralysis, convulsions, bronchial constriction, and
death by asphyxiation. Organophosphates (OP), esters
of phosphoric acid, are a class of irreversible AChE
inhibitors.[21] Cleavage of OP by AChE leaves a phosphoryl group in the esteratic site, which is slow to
be hydrolyzed (on the order of days) and can become
covalently bound. Irreversible AChE inhibitors have
been used in insecticides (e.g., malathion) and nerve
gases for chemical warfare (e.g., Sarin and Soman).
Carbamates, esters of N-methyl carbamic acid, are
AChE inhibitors that hydrolyze in hours and have been
used for medical purposes (e.g., physostigmine for the
treatment of glaucoma). Reversible inhibitors occupy
the esteratic site for short periods of time (seconds
to minutes) and are used to treat of a range of central nervous system diseases. Tetrahydroaminoacridine
(THA) and donepezil are FDA-approved to improve cognitive function in Alzheimers disease. Rivastigmine
is also used to treat Alzheimers and Lewy body dementia, and pyridostigmine bromide is used to treat
myasthenia gravis.[22][23][24][25][26][27] Alzheimer disease
drugs donepezil, galantamine, and rivastigmine are inhibitors of acetylcholinesterase as well.[15][28]

In mammals, acetylcholinesterase is encoded by a single AChE gene while some invertebrates have multiple acetylcholinesterase genes. Diversity in the transcribed products from the sole mammalian gene arises
from alternative mRNA splicing and post-translational
associations of catalytic and structural subunits. There
are three known forms: T (tail), R (read through), and
H(hydrophobic).[35]

5.1 AChET
The major form of acetylcholinesterase found in brain,
muscle, and other tissues, known as is the hydrophilic
species, which forms disulde-linked oligomers with
collagenous, or lipid-containing structural subunits. In
the neuromuscular junctions AChE expresses in asymmetric form which associates with ColQ or subunit. In the
central nervous system it is associated with PRiMA which
stands for Proline Rich Membrane anchor to form symmetric form. In either case, the ColQ or PRiMA anchor
serves to maintain the enzyme in the intercellular junction, ColQ for the neuromuscular junction and PRiMA
for synapses.

5.2 AChEH

The other, alternatively-spliced form expressed primarily in the erythroid tissues, diers at the Cterminus, and contains a cleavable hydrophobic peptide
with a PI-anchor site. It associates with membranes
through the phosphoinositide (PI) moieties added postAn endogenous inhibitor of AChE in neurons is Mir-132 translationally.[36]
microRNA, which may limit inammation in the brain by
silencing the expression of this protein and allowing ACh
to act in an anti-inammatory capacity.[29]
5.3 AChER
It has also been shown that the main active ingredient in
cannabis, tetrahydrocannabinol, is a competitive inhibitor The third type has, so far, only been found in Torpedo sp.
of acetylcholinesterase.[30]
and mice although it is hypothesized in other species. It is

3
thought to be involved in the stress response and, possibly,
inammation.[37]

See also
Acetylcholinesterase inhibitor
Cholinesterases
Proteopedia Acetylcholinesterase

References

[1] Katzung BG (2001). Basic and clinical pharmacology:

Introduction to autonomic pharmacology (8 ed.). The McGraw Hill Companies. pp. 7591. ISBN 978-0-07160405-5.
[2] Quinn DM (1987). Acetylcholinesterase: enzyme
structure, reaction dynamics, and virtual transition states.
Chemical Review 87 (5): 95579.
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[3] Taylor P, Radi Z (1994).
The cholinesterases:
from genes to proteins.
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[4] Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L et al. (August 1991). Atomic
structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253 (5022): 8729. Bibcode:1991Sci...253..872S.
doi:10.1126/science.1678899. PMID 1678899.
[5] Sussman JL, Harel M, Silman I (June 1993). Threedimensional structure of acetylcholinesterase and of
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[6] Radi Z, Gibney G, Kawamoto S, MacPhee-Quigley K,
Bongiorno C, Taylor P (October 1992). Expression of
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[7] Ordentlich A, Barak D, Kronman C, Ariel N, Segall Y,
Velan B et al. (February 1995). Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite
tryptophan 86 to catalytic eciency and allosteric modulation of acetylcholinesterase. J. Biol. Chem. 270 (5):
208291. doi:10.1074/jbc.270.5.2082. PMID 7836436.
[8] Ariel N, Ordentlich A, Barak D, Bino T, Velan B, Shafferman A (October 1998). The 'aromatic patch' of three
proximal residues in the human acetylcholinesterase active centre allows for versatile interaction modes with inhibitors. Biochem. J. 335 (1): 95102. PMC 1219756.
PMID 9742217.

[9] Ordentlich A, Barak D, Kronman C, Flashner Y, Leitner M, Segall Y et al. (August 1993). Dissection of the
human acetylcholinesterase active center determinants of
substrate specicity. Identication of residues constituting the anionic site, the hydrophobic site, and the acyl
pocket. J. Biol. Chem. 268 (23): 1708395. PMID
8349597.
[10] Tougu V (2001). Acetylcholinesterase: Mechanism
of Catalysis and Inhibition. Current Medicinal Chemistry Central Nervous System Agents 1 (2): 155170.
doi:10.2174/1568015013358536.
[11] Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C et al. (1993). Quaternary ligand
binding to aromatic residues in the active-site gorge
of acetylcholinesterase. Proceedings of the National
Academy of Sciences of the United States of America 90 (19): 90315. Bibcode:1993PNAS...90.9031H.
doi:10.1073/pnas.90.19.9031. PMC 47495. PMID
8415649.
[12] Tripathi A (October 2008). Acetylcholinsterase: A Versatile Enzyme of Nervous System. Annals of Neuroscience 15 (4). doi:10.5214/ans.0972.7531.2008.150403.
[13] Pauling L (1946). Molecular Architecture and Biological
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[14] Fersht A (1985). Enzyme structure and mechanism. San
Francisco: W.H. Freeman. p. 14. ISBN 0-7167-1614-3.
[15] Pohanka M (2011). Cholinesterases, a target of pharmacology and toxicology. Biomedical Papers Olomouc
155 (3): 219229. doi:10.5507/bp.2011.036. PMID
22286807.
[16] Pohanka M (2012). Alpha7 nicotinic acetylcholine receptor is a target in pharmacology and toxicology. Int
J Mol Sci 13 (2): 221938. doi:10.3390/ijms13022219.
PMC 3292018. PMID 22408449.
[17] Whittaker VP (1990). The Contribution of Drugs
and Toxins to Understanding of Cholinergic Function. Trends in Physiological Sciences 11 (1): 813.
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[18] Purves D; George J. Augustine, David Fitzpatrick,
William C. Hall, Anthony-Samuel LaMantia, James O.
McNamara, Leonard E. White (2008). Neuroscience 4th
ed. Sinauer Associates. pp. 1212. ISBN 978-0-87893697-7.
[19] Pohanka M (2012). Alpha7 Nicotinic Acetylcholine
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[20] [citation needed]
[21] National Pesticide Information Center-Diazinon Technical Fact Sheet. Retrieved 24 February 2012.
[22] Clinical Application: Acetylcholine and Alzheimers
Disease. Retrieved 24 February 2012.

8 FURTHER READING

[23] Stoelting, R.K. (1999). Anticholinesterase Drugs and

Cholinergic Agonists, in Pharmacology and Physiology
in Anesthetic Practice. Lippincott-Raven. ISBN 978-07817-5469-9.

[35] Massouli J, Perrier N, Noureddine H, Liang D,

Bon S (2008).
Old and new questions about
cholinesterases. Chem Biol Interact 175 (13): 3044.
doi:10.1016/j.cbi.2008.04.039. PMID 18541228.

[24] Taylor, P; Hardman, J.G, Limbird, L.E, Molino, P.B.,

Ruddon, R.W, Gilman, A.G.,eds (1996). 5: Autonomic
Pharmacology: Cholinergic Drugs. The Pharmacologial
Basis of Therapeutics. THe McGraw-Hill Companies. pp.
161174. ISBN 978-0-07-146804-6.

[36] Entrez Gene: ACHE acetylcholinesterase (Yt blood

group)".

[25] Blumenthal D, Brunton L, Goodman LS, Parker K,

Gilman A, Lazo JS, Buxton I (1996). 5: Autonomic Pharmacology: Cholinergic Drugs. Goodman &
Gilmans The pharmacological basis of therapeutics. New
York: McGraw-Hill. p. 1634. ISBN 978-0-07-1468046.
[26] Drachman, D.B.; Isselbacher, K.J., Braunwald, E., Wilson, J.D., Martin, J.B., Fauci, A.S. Kasper, D.L., eds
(1998). Harrisons Principles of Internal Medicine (14
ed.). The McCraw-Hill Companies. pp. 24692472.
ISBN 978-0-07-020291-7.
[27] Rae, RB. Autonomic and Somatic Nervous Systems in
Netters Illustrated Pharmacology. Elsevier Health Science. p. 43. ISBN 978-1-929007-60-8.
[28] Pohanka M (2011). Alzheimers disease and related neurodegenerative disorders: implication and counteracting
of melatonin. Journal of Applied Biomedicine 9 (4):
185196. doi:10.2478/v10136-011-0003-6.
[29] Shaked I, Meerson A, Wolf Y, Avni R, Greenberg D,
Gilboa-Geen A et al. (2009). MicroRNA-132 potentiates cholinergic anti-inammatory signaling by targeting acetylcholinesterase. Immunity 31 (6): 96573.
doi:10.1016/j.immuni.2009.09.019. PMID 20005135.
[30] Eubanks LM, Rogers CJ, Beuscher AE, Koob GF, Olson AJ, Dickerson TJ et al. (2006). A molecular
link between the active component of marijuana and
Alzheimers disease pathology. Mol Pharm 3 (6): 773
7. doi:10.1021/mp060066m. PMC 2562334. PMID
17140265.
[31] Massouli J, Pezzementi L, Bon S, Krejci E, Vallette
FM (July 1993). Molecular and cellular biology of
cholinesterases. Progress in Neurobiology 41 (1): 3191.
doi:10.1016/0301-0082(93)90040-Y. PMID 8321908.
[32] Chacko LW, Cerf JA (1960). Histochemical localization
of cholinesterase in the amphibian spinal cord and alterations following ventral root section. Journal of Anatomy
94 (Pt 1): 7481. PMC 1244416. PMID 13808985.
[33] Koelle GB (1954). The histochemical localization of
cholinesterases in the central nervous system of the
rat. Journal of Comparative Anatomy 100 (1): 21135.
doi:10.1002/cne.901000108. PMID 13130712.
[34] Bartels CF, Zelinski T, Lockridge O (May 1993).
Mutation at codon 322 in the human acetylcholinesterase
(ACHE) gene accounts for YT blood group polymorphism. Am. J. Hum. Genet. 52 (5): 92836. PMC
1682033. PMID 8488842.

[37] Dori A, Ifergane G, Saar-Levy T, Bersudsky M, Mor I,

Soreq H et al. (2007). Readthrough acetylcholinesterase
in inammation-associated neuropathies.
Life Sci
80 (2425): 236974. doi:10.1016/j.lfs.2007.02.011.
PMID 17379257.

8 Further reading
Silman I, Futerman AH (1988). Modes of attachment of acetylcholinesterase to the surface membrane. Eur. J. Biochem. 170 (12): 1122.
doi:10.1111/j.1432-1033.1987.tb13662.x. PMID
3319614.
Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L et al. (1991). Atomic structure
of acetylcholinesterase from Torpedo californica: a
prototypic acetylcholine-binding protein. Science
253 (5022): 8729. Bibcode:1991Sci...253..872S.
doi:10.1126/science.1678899. PMID 1678899.
Soreq H, Seidman S (2001). Acetylcholinesterase-new roles for an old actor. Nature Reviews Neuroscience 2 (4): 294302. doi:10.1038/35067589.
PMID 11283752.
Shen T, Tai K, Henchman RH, McCammon
JA (2003).
Molecular dynamics of acetylcholinesterase. Acc. Chem. Res. 35 (6): 33240.
doi:10.1021/ar010025i. PMID 12069617.
Pakaski M, Kasa P (2003). Role of acetylcholinesterase inhibitors in the metabolism of
amyloid precursor protein. Current drug targets. CNS and neurological disorders 2 (3): 163
71.
doi:10.2174/1568007033482869.
PMID
12769797.
Meshorer E, Soreq H (2006). Virtues and woes
of AChE alternative splicing in stress-related neuropathologies. Trends Neurosci. 29 (4): 21624.
doi:10.1016/j.tins.2006.02.005. PMID 16516310.
Ehrlich G, Viegas-Pequignot E, Ginzberg D, Sindel L, Soreq H, Zakut H (1992). Mapping the human acetylcholinesterase gene to chromosome 7q22
by uorescent in situ hybridization coupled with selective PCR amplication from a somatic hybrid
cell panel and chromosome-sorted DNA libraries.
Genomics 13 (4): 11927. doi:10.1016/08887543(92)90037-S. PMID 1380483.

5
Spring FA, Gardner B, Anstee DJ (1992). Evidence that the antigens of the Yt blood group
system are located on human erythrocyte acetylcholinesterase. Blood 80 (8): 213641. PMID
1391965.

Bazelyansky M, Robey E, Kirsch JF (1986). Fractional diusion-limited component of reactions catalyzed by acetylcholinesterase. Biochemistry 25
(1): 12530. doi:10.1021/bi00349a019. PMID
3954986.

Shaerman A, Kronman C, Flashner Y, Leitner M,

Grosfeld H, Ordentlich A et al. (1992). Mutagenesis of human acetylcholinesterase. Identication of residues involved in catalytic activity and in
polypeptide folding. J. Biol. Chem. 267 (25):
176408. PMID 1517212.

Gaston SM, Marchase RB, Jakoi ER (1982). Brain

ligatin: a membrane lectin that binds acetylcholinesterase. J. Cell. Biochem. 18 (4): 447
59. doi:10.1002/jcb.1982.240180406. PMID
7085778.

Getman DK, Eubanks JH, Camp S, Evans GA, Taylor P (1992). The human gene encoding acetylcholinesterase is located on the long arm of chromosome 7. Am. J. Hum. Genet. 51 (1): 1707.
PMC 1682883. PMID 1609795.
Li Y, Camp S, Rachinsky TL, Getman D, Taylor
P (1992). Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissuespecic expression. J. Biol. Chem. 266 (34):
2308390. PMID 1744105.
Velan B, Grosfeld H, Kronman C, Leitner M, Gozes
Y, Lazar A et al. (1992). The eect of elimination
of intersubunit disulde bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase
Cys-580----Ala mutant. J. Biol. Chem. 266 (35):
2397784. PMID 1748670.
Soreq H, Ben-Aziz R, Prody CA, Seidman S, Gnatt
A, Neville L et al. (1991). Molecular cloning
and construction of the coding region for human
acetylcholinesterase reveals a G + C-rich attenuating structure. Proceedings of the National Academy
of Sciences of the United States of America 87
(24): 968892. Bibcode:1990PNAS...87.9688S.
doi:10.1073/pnas.87.24.9688. PMC 55238. PMID
2263619.
Chhajlani V, Derr D, Earles B, Schmell E, August T (1989). Purication and partial amino
acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 247 (2): 279
82. doi:10.1016/0014-5793(89)81352-3. PMID
2714437.
Lapidot-Lifson Y, Prody CA, Ginzberg D, Meytes
D, Zakut H, Soreq H (1989). Coamplication
of human acetylcholinesterase and butyrylcholinesterase genes in blood cells: correlation with
various leukemias and abnormal megakaryocytopoiesis. Proceedings of the National Academy
of Sciences of the United States of America 86
(12): 47159. Bibcode:1989PNAS...86.4715L.
doi:10.1073/pnas.86.12.4715.
PMC 287342.
PMID 2734315.

Ordentlich A, Barak D, Kronman C, Ariel N, Segall

Y, Velan B et al. (1995). Contribution of aromatic
moieties of tyrosine 133 and of the anionic subsite
tryptophan 86 to catalytic eciency and allosteric
modulation of acetylcholinesterase. J. Biol. Chem.
270 (5): 208291. doi:10.1074/jbc.270.5.2082.
PMID 7836436.
Maruyama K, Sugano S (1994). Oligo-capping:
a simple method to replace the cap structure
of eukaryotic mRNAs with oligoribonucleotides.
Gene 138 (12): 1714.
doi:10.1016/03781119(94)90802-8. PMID 8125298.
Ben Aziz-Aloya R, Sternfeld M, Soreq H (1994).
Promoter elements and alternative splicing in the
human ACHE gene. Prog. Brain Res. 98: 147
53. doi:10.1016/s0079-6123(08)62392-4. PMID
8248502.
Massouli J, Pezzementi L, Bon S, Krejci E, Vallette FM (1993). Molecular and Cellular Biology of Cholinesterases. Prog. Brain Res. 41
(1): 3191. doi:10.1016/0301-0082(93)90040-Y.
PMID 8321908.

9 External links
ATSDR Case Studies in Environmental Medicine:
Cholinesterase Inhibitors, Including Insecticides and Chemical Warfare Nerve Agents U.S.
Department of Health and Human Services
Proteopedia Acetylcholinesterase
Proteopedia AChE_inhibitors_and_substrates
Proteopedia AChE_inhibitors_and_substrates_(Part_II)
Proteopedia
AChE
bivalent
inhibitors
AChE_bivalent_inhibitors AChE bivalent inhibitors
Acetylcholinesterase: A gorge-ous enzyme QUite
Interesting PDB Structure article at PDBe

10

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