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PDBsum entry 5hm2
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DOI no:
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Peerj
4:e1964
(2016)
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PubMed id:
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Crystal structure of the 3C protease from Southern African Territories type 2 foot-and-mouth disease virus.
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J.Yang,
E.N.Leen,
F.F.Maree,
S.Curry.
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ABSTRACT
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The replication of foot-and-mouth disease virus (FMDV) is dependent on the
virus-encoded 3C protease (3C(pro)). As in other picornaviruses, 3C(pro)
performs most of the proteolytic processing of the polyprotein expressed from
the large open reading frame in the RNA genome of the virus. Previous work
revealed that the 3C(pro) from serotype A-one of the seven serotypes of
FMDV-adopts a trypsin-like fold. On the basis of capsid sequence comparisons the
FMDV serotypes are grouped into two phylogenetic clusters, with O, A, C, and
Asia 1 in one, and the three Southern African Territories serotypes, (SAT-1,
SAT-2 and SAT-3) in another, a grouping pattern that is broadly, but not
rigidly, reflected in 3C(pro) amino acid sequences. We report here the cloning,
expression and purification of 3C proteases from four SAT serotype viruses
(SAT2/GHA/8/91, SAT1/NIG/5/81, SAT1/UGA/1/97, and SAT2/ZIM/7/83) and the crystal
structure at 3.2 Å resolution of 3C(pro) from SAT2/GHA/8/91.
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}
}
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