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PDBsum entry 4it7
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Hydrolase inhibitor
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PDB id
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4it7
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References listed in PDB file
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Key reference
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Title
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Structural basis for the immunomodulatory function of cysteine protease inhibitor from human roundworm ascaris lumbricoides.
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Authors
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G.Mei,
J.Dong,
Z.Li,
S.Liu,
Y.Liu,
M.Sun,
G.Liu,
Z.Su,
J.Liu.
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Ref.
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Plos One, 2014,
9,
e96069.
[DOI no: ]
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PubMed id
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Abstract
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Immunosuppression associated with infections of nematode parasites has been
documented. Cysteine protease inhibitor (CPI) released by the nematode parasites
is identified as one of the major modulators of host immune response. In this
report, we demonstrated that the recombinant CPI protein of Ascaris lumbricoides
(Al-CPI) strongly inhibited the activities of cathepsin L, C, S, and showed
weaker effect to cathepsin B. Crystal structure of Al-CPI was determined to 2.1
Å resolution. Two segments of Al-CPI, loop 1 and loop 2, were proposed as the
key structure motifs responsible for Al-CPI binding with proteases and its
inhibitory activity. Mutations at loop 1 and loop 2 abrogated the protease
inhibition activity to various extents. These results provide the molecular
insight into the interaction between the nematode parasite and its host and will
facilitate the development of anthelmintic agents or design of anti-autoimmune
disease drugs.
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