4AIG

ADAMALYSIN II WITH PHOSPHONATE INHIBITOR

Summary for 4AIG

• Entry DOI: 10.2210/pdb4aig/pdb
• Descriptor: ADAMALYSIN II, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: snake venom metalloendopeptidase, zinc protease, metalloendopeptidase
• Biological source: Crotalus adamanteus (eastern diamondback rattlesnake)
• Cellular location: Secreted: P34179
• Total number of polymer chains: 1
• Total formula weight: 23594.30

Authors

Pochetti, G.,Mazza, F.,Gavuzzo, E.,Cirilli, M. (deposition date: 1997-10-16, release date: 1998-11-11, Last modification date: 2024-10-16)

Primary citation

Cirilli, M.,Gallina, C.,Gavuzzo, E.,Giordano, C.,Gomis-Ruth, F.X.,Gorini, B.,Kress, L.F.,Mazza, F.,Paradisi, M.P.,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., 418:319-322, 1997

PubMed 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-alpha-converting enzyme (TACE) reveals a smaller S1' pocket for this enzyme.

PubMed: 9428736
DOI: 10.1016/S0014-5793(97)01401-4

Experimental method

X-RAY DIFFRACTION (2 Å)