Send to

Choose Destination
FEBS Lett. 1993 Sep 27;331(1-2):134-40.

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'.

Author information

Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried (bei München), Germany.


The X-ray crystal structures of two zinc endopeptidases, astacin from crayfish, and adamalysin II from snake venom, reveal a strong overall topological equivalence and virtually identical extended HEXXHXXGXXH zinc-binding segments, but in addition a methionine-containing turn of similar conformation (the 'Met-turn'), which forms a hydrophobic basis for the zinc ion and the three liganding histidine residues. These two features are also present in a similar arrangement in the matrix metalloproteinases (matrixins) and in the large bacterial Serratia proteinase-like peptidases (serralysins). We suggest that these four proteinases represent members of distinct subfamilies which can be grouped together in a family, for which we propose the designation, metzincins.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center