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PDBsum entry 3ebn
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References listed in PDB file
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Key reference
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Title
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C-Terminal domain of sars-Cov main protease can form a 3d domain-Swapped dimer.
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Authors
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N.Zhong,
S.Zhang,
F.Xue,
X.Kang,
P.Zou,
J.Chen,
C.Liang,
Z.Rao,
C.Jin,
Z.Lou,
B.Xia.
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Ref.
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Protein Sci, 2009,
18,
839-844.
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PubMed id
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Abstract
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SARS coronavirus main protease (M(pro)) plays an essential role in the extensive
proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an
important target for anti-SARS drug development. We have reported that both the
M(pro) C-terminal domain alone (M(pro)-C) and the N-finger deletion mutant of
M(pro) (M(pro)-Delta7) exist as a stable dimer and a stable monomer (Zhong et
al., J Virol 2008; 82:4227-4234). Here, we report structures of both M(pro)-C
monomer and dimer. The structure of the M(pro)-C monomer is almost identical to
that of the C-terminal domain in the crystal structure of M(pro). Interestingly,
the M(pro)-C dimer structure is characterized by 3D domain-swapping, in which
the first helices of the two protomers are interchanged and each is enwrapped by
four other helices from the other protomer. Each folding subunit of the M(pro)-C
domain-swapped dimer still has the same general fold as that of the M(pro)-C
monomer. This special dimerization elucidates the structural basis for the
observation that there is no exchange between monomeric and dimeric forms of
M(pro)-C and M(pro)-Delta7.
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