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’

作者：Wolfram Bode, F. Xavier Gomis‐Rüth, Walter Stöckler · 发表于：FEBS Letters · 年份：1993 · DOI：10.1016/0014-5793(93)80312-i · 被引用次数：763 · 研究领域：Venomous Animal Envenomation and Studies、Protease and Inhibitor Mechanisms、Biochemical and Structural Characterization

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.