4aig
From Proteopedia
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'''ADAMALYSIN II WITH PHOSPHONATE INHIBITOR''' | '''ADAMALYSIN II WITH PHOSPHONATE INHIBITOR''' | ||
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[[Category: Mazza, F.]] | [[Category: Mazza, F.]] | ||
[[Category: Pochetti, G.]] | [[Category: Pochetti, G.]] | ||
| - | [[Category: | + | [[Category: Snake venom metalloendopeptidase]] |
| - | [[Category: | + | [[Category: Zinc protease]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:20:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:20, 4 May 2008
ADAMALYSIN II WITH PHOSPHONATE INHIBITOR
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. 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 Page seeded by OCA on Sun May 4 22:20:29 2008
