Structural highlights
Function
VM12_CROAD Has no significant hemorrhagic activity, but inactivates serpins by limited proteolysis of their reactive-site loops.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The search of reprolysin inhibitors offers the possibility of intervention against both matrixins and ADAMs. Here we report the crystal structure of the complex between adamalysin II, a member of the reprolysin family, and a phosphonate inhibitor modeled on an endogenous venom tripeptide. The inhibitor occupies the primed region of the cleavage site adopting a retro-binding mode. The phosphonate group ligates the zinc ion in an asymmetric bidentate mode and the adjacent Trp indole system partly fills the primary specificity subsite S1'. An adamalysin-based model of tumor necrosis factor-alpha-converting enzyme (TACE) reveals a smaller S1' pocket for this enzyme.
2 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode.,Cirilli M, Gallina C, Gavuzzo E, Giordano C, Gomis-Ruth FX, Gorini B, Kress LF, Mazza F, Paradisi MP, Pochetti G, Politi V FEBS Lett. 1997 Dec 1;418(3):319-22. PMID:9428736[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cirilli M, Gallina C, Gavuzzo E, Giordano C, Gomis-Ruth FX, Gorini B, Kress LF, Mazza F, Paradisi MP, Pochetti G, Politi V. 2 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode. FEBS Lett. 1997 Dec 1;418(3):319-22. PMID:9428736
