Wolfram Bode

TL;DR: Recently determined crystal structures of chicken cystatin and human stefin B established a new mechanism of interaction between cysteine proteinases and their inhibitors which is fundamentally different from the standard mechanism for serine proteinase inhibitors and their inhibitor.

TL;DR: 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.

TL;DR: The crystallographic structure of a recombinant hirudin-thrombin complex has been solved at 2.3 angstrom (A) resolution and abundant interactions may account for the high affinity and specificity of hirUDin.

TL;DR: The corresponding four distinct families of zinc peptidases, the astacins, the matrix metalloproteinases (matrixins, collagenases), the adamalysins/reprolysins (snake venom proteinases/reproductive tract proteins), and the serralysins appear to have originated by divergent evolution from a common ancestor and form a superfamily of proteolytic enzymes for which the designation “metzincins” has been proposed.