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PDBsum entry 4fvb
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References listed in PDB file
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Key reference
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Title
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Conformational plasticity of the 2a proteinase from enterovirus 71.
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Authors
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Q.Cai,
M.Yameen,
W.Liu,
Z.Gao,
Y.Li,
X.Peng,
Y.Cai,
C.Wu,
Q.Zheng,
J.Li,
T.Lin.
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Ref.
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J Virol, 2013,
87,
7348-7356.
[DOI no: ]
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PubMed id
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Abstract
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The 2A proteinase (2A(pro)) is an enterovirally encoded cysteine protease that
plays essential roles in both the processing of viral precursor polyprotein and
the hijacking of host cell translation and other processes in the virus life
cycle. Crystallographic studies of 2A(pro) from enterovirus 71 (EV71) and its
interaction with the substrate are reported here. EV71 2A(pro) was comprised of
an N-terminal domain of a four-stranded antiparallel β sheet and a C-terminal
domain of a six-stranded antiparallel β barrel with a tightly bound zinc atom.
Unlike in other 2A(pro) structures, there is an open cleft across the surface of
the protein in an open conformation. As demonstrated by the crystallographic
studies and modeling of the complex structure, the open cleft could be fitted
with the substrate. On comparison 2A(pro) of EV71 to those of the human
rhinovirus 2 and coxsackievirus B4, the open conformation could be closed with a
hinge motion in the bII2 and cII β strands. This was supported by molecular
dynamic simulation. The structural variation among different 2A(pro) structures
indicates a conformational flexibility in the substrate-binding cleft. The open
structure provides an accessible framework for the design and development of
therapeutics against the viral target.
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