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PDBsum entry 4doq
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Hydrolase/hydrolase inhibitor
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PDB id
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4doq
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References listed in PDB file
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Key reference
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Title
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Structure basis 1/2slpi and porcine pancreas trypsin interaction.
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Authors
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K.Fukushima,
T.Kamimura,
M.Takimoto-Kamimura.
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Ref.
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J Synchrotron Radiat, 2013,
20,
943-947.
[DOI no: ]
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PubMed id
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Abstract
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SLPI (secretory leukocyte protease inhibitor) is a 107-residue protease
inhibitor which inhibits various serine proteases, including elastase,
cathepsin G, chymotrypsin and trypsin. SLPI is obtained as a multiple
inhibitor in lung defense and in chronic airway infection. X-ray crystal
structures have so far reported that they are full-length SLPIs with bovine
α-chymotrypsin and 1/2SLPI (recombinant C-terminal domain of SLPI;
Arg58-Ala107) with HNE (human neutrophil elastase). To understand the role of
this multiple inhibitory mechanism, the crystal structure of 1/2SLPI with
porcine pancreas trypsin was solved and the binding modes of two other complexes
compared. The Leu residue surprisingly interacts with the S1 site of trypsin, as
with chymotrypsin and elastase. The inhibitory mechanism of 1/2SLPI using the
wide primary binding site contacts (from P2' to P5) with various serine
proteases is discussed. These inhibitory mechanisms have been acquired in the
evolution of the protection system for acute inflammatory diseases.
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