4j4m
Crystal structure of TM-1, a Trimeresurus mucrosquamatus venom metalloproteinase
Structural highlights
FunctionVM1T1_PROMU Potent fibrinogenolytic protease which cleaves mainly the Aalpha (FGA) and Bbeta (FGB) chains of fibrinogen and slightly the gamma chain (FGG) (PubMed:7488093, PubMed:8193588). Shows preference for substrates having a moderate-size and hydrophobic residue at the P1' position. Preferentially cleaves Ala-|-Leu and Tyr-|-Leu bonds (PubMed:23732127). Is more susceptible to tripeptide inhibitors than TM-3 (AC O57413) (PubMed:9703966).[1] [2] [3] [4] Publication Abstract from PubMedThe 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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