4J4M

Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors.

(2013) Toxicon 71C: 140-146

• PubMed: 23732127 Search on PubMed
• DOI: https://doi.org/10.1016/j.toxicon.2013.05.009
• Primary Citation of Related Structures:  
  4J4M


• PubMed 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.

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Organizational Affiliation: 

Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan.