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PDBsum entry 1vzj
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26 a.a.
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31 a.a.
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32 a.a.
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27 a.a.
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34 a.a.
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15 a.a.
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References listed in PDB file
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Key reference
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Title
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The synaptic acetylcholinesterase tetramer assembles around a polyproline ii helix.
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Authors
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H.Dvir,
M.Harel,
S.Bon,
W.Q.Liu,
M.Vidal,
C.Garbay,
J.L.Sussman,
J.Massoulié,
I.Silman.
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Ref.
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EMBO J, 2004,
23,
4394-4405.
[DOI no: ]
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PubMed id
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Abstract
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Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and
brain depends on interaction of the tryptophan amphiphilic tetramerization (WAT)
sequence, at the C-terminus of its major splice variant (T), with a proline-rich
attachment domain (PRAD), of the anchoring proteins, collagenous (ColQ) and
proline-rich membrane anchor. The crystal structure of the WAT/PRAD complex
reveals a novel supercoil structure in which four parallel WAT chains form a
left-handed superhelix around an antiparallel left-handed PRAD helix resembling
polyproline II. The WAT coiled coils possess a WWW motif making repetitive
hydrophobic stacking and hydrogen-bond interactions with the PRAD. The WAT
chains are related by an approximately 4-fold screw axis around the PRAD. Each
WAT makes similar but unique interactions, consistent with an asymmetric pattern
of disulfide linkages between the AChE tetramer subunits and ColQ. The P59Q
mutation in ColQ, which causes congenital endplate AChE deficiency, and is
located within the PRAD, disrupts crucial WAT-WAT and WAT-PRAD interactions. A
model is proposed for the synaptic AChE(T) tetramer.
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Figure 1.
Figure 1 Schematic representations of AChE tetramers. (A) Modes
of assembly of AChE subunits into tetramers. (B) Orientations of
the polypeptide chains and arrangement of disulfide bonds in the
[AChE[T]][4]ColQ complex deduced by site-directed mutagenesis.
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Figure 7.
Figure 7 Stacking interactions between the WAT and PRAD helices.
Side view of the complex, with the superhelical axis running
vertically, and PRAD depicted as a stick model. Only the Trps of
WAT are shown, in space-filling format, with those of each WAT
chain colored individually. The Trp side chains form a spiral
staircase around the PRAD, fitting into grooves formed by the
extended left-handed PRAD helix.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2004,
23,
4394-4405)
copyright 2004.
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