4aig | pdb_00004aig
ADAMALYSIN II WITH PHOSPHONATE INHIBITOR
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Overview
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.
About this Structure
4AIG is a Single protein structure of sequence from Crotalus adamanteus with ZN, CA and FLX as ligands. Active as Adamalysin, with EC number 3.4.24.46 Full crystallographic information is available from OCA.
Reference
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
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