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- W2041279071 abstract "The crystal structure of TM-1, a P-I class snake-venom metalloproteinase (SVMP) from the Trimeresurus mucrosquamatus venom, was determined at 1.8-Å resolution. The structure exhibits the typical feature of SVMPs and is stabilized by three disulfide linkages. The active site shows a deep S1′ substrate-binding pocket limited by the non-conserved Pro174 at the bottom. Further comparisons with other SVMPs suggest that the deep S1′ site of TM-1 correlates with its high inhibition sensitivity to the endogenous tripeptide inhibitors. Proteolytic specificity analysis revealed that TM-1 prefers substrates having a moderate-size and hydrophobic residue at the P1′ position, consistent with our structural observation." @default.
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- W2041279071 date "2013-09-01" @default.
- W2041279071 modified "2023-09-27" @default.
- W2041279071 title "Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors" @default.
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- W2041279071 doi "https://doi.org/10.1016/j.toxicon.2013.05.009" @default.
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