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

Tsung Lin Chou, Cheng Heng Wu, Kai Fa Huang, Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)140-146
Number of pages7
JournalToxicon
Volume71
DOIs
Publication statusPublished - Sep 1 2013
Externally publishedYes

Keywords

  • S1' substrate-binding pocket
  • Snake-venom metalloproteinase
  • Trimeresurus mucrosquamatus
  • Tripeptide inhibitor

ASJC Scopus subject areas

  • Toxicology

Fingerprint

Dive into the research topics of 'Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors'. Together they form a unique fingerprint.

Cite this