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PDBsum entry 4kts
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Hydrolase/hydrolase inhibitor
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PDB id
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4kts
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References listed in PDB file
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Key reference
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Title
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Harnessing the evolvability of tricyclic microviridins to dissect protease-Inhibitor interactions.
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Authors
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A.R.Weiz,
K.Ishida,
F.Quitterer,
S.Meyer,
J.C.Kehr,
K.M.Müller,
M.Groll,
C.Hertweck,
E.Dittmann.
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Ref.
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Angew Chem Int Ed Engl, 2014,
53,
3735-3738.
[DOI no: ]
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PubMed id
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Abstract
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Understanding and controlling proteolysis is an important goal in therapeutic
chemistry. Among the natural products specifically inhibiting proteases
microviridins are particularly noteworthy. Microviridins are ribosomally
produced and posttranslationally modified peptides that are processed into a
unique, cagelike architecture. Here, we report a combined rational and random
mutagenesis approach that provides fundamental insights into
selectivity-conferring moieties of microviridins. The potent variant
microviridin J was co-crystallized with trypsin, and for the first time the
three-dimensional structure of microviridins was determined and the mode of
inhibition revealed.
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