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PDBsum entry 1m93
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Viral protein
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PDB id
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1m93
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of viral serpin crma provides insights into its mechanism of cysteine proteinase inhibition.
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Authors
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M.Simonovic,
Gettins pgw,
K.Volz.
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Ref.
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Protein Sci, 2000,
9,
1423-1427.
[DOI no: ]
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PubMed id
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Abstract
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CrmA is an unusual viral serpin that inhibits both cysteine and serine
proteinases involved in the regulation of host inflammatory and apoptosis
processes. It differs from other members of the serpin superfamily by having a
reactive center loop that is one residue shorter, and by its apparent inability
to form SDS-stable covalent complexes with cysteine proteinases. To obtain
insight into the inhibitory mechanism of crmA, we determined the crystal
structure of reactive center loop-cleaved crmA to 2.9 A resolution. The
structure, which is the first of a viral serpin, suggests that crmA can inhibit
cysteine proteinases by a mechanism analogous to that used by other serpins
against serine proteinases. However, one striking difference from other serpins,
which may be significant for in vivo function, is an additional highly charged
antiparallel strand for b sheet A, whose sequence and length are unique to crmA.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray diffraction analysis of a recombinant cysteine-Free mutant of crma.
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Authors
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M.Simonovic,
P.G.Gettins,
K.Volz.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
1440-1442.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2 (a) A crystal cluster and (b) a single crystal of the
cysteine-free mutant of crmA (same scale). Crystals were formed
over a month by the hanging-drop vapour-diffusion method when
drops were equilibrated against 1 ml 0.1 M Na HEPES pH 7.50,
1.6 M Na/KH[2]PO[4]. The crystal in (b) was 150 µm long.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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