Crystal structure of cathepsin A, a novel target for the treatment of cardiovascular diseases

- The structures of active cathepsin A and the inactive precursor are very similar.
- The only major difference is the absence of a 40 residue activation domain.
- The termini of the active catalytic core are held together by a disulfide bond.
- Compound 1 reacts with the catalytic Ser150, building a tetrahedral intermediate.
- Compound 2 is cleaved by the enzyme and a fragment remained bound.