2 Å X‐ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro‐binding mode
- 12 December 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 418 (3) , 319-322
- https://doi.org/10.1016/s0014-5793(97)01401-4
Abstract
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-α-converting enzyme (TACE) reveals a smaller S1′ pocket for this enzyme.Keywords
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