Structural highlights
Publication Abstract from PubMed
The crystal structure of TM-1, a P-I class snake-venom metalloproteinase (SVMP) from the Trimeresurus mucrosquamatus venom, was determined at 1.8-A 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.
Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors.,Chou TL, Wu CH, Huang KF, Wang AH Toxicon. 2013 Sep;71:140-6. doi: 10.1016/j.toxicon.2013.05.009. Epub 2013 May 31. PMID:23732127[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chou TL, Wu CH, Huang KF, Wang AH. Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors. Toxicon. 2013 Sep;71:140-6. doi: 10.1016/j.toxicon.2013.05.009. Epub 2013 May 31. PMID:23732127 doi:10.1016/j.toxicon.2013.05.009
