Structural highlights
Function
[CYSP_TRYCR] Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group. The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structures of two hydroxymethyl ketone inhibitors complexed to the cysteine protease cruzain have been determined at 1.1 and 1.2 A resolution, respectively. These high resolution crystal structures provide the first structures of non-covalent inhibitors bound to cruzain. A series of compounds were prepared and tested based upon the structures providing further insight into the key binding interactions.
Crystal structures of reversible ketone-Based inhibitors of the cysteine protease cruzain.,Huang L, Brinen LS, Ellman JA Bioorg Med Chem. 2003 Jan 2;11(1):21-9. PMID:12467703[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huang L, Brinen LS, Ellman JA. Crystal structures of reversible ketone-Based inhibitors of the cysteine protease cruzain. Bioorg Med Chem. 2003 Jan 2;11(1):21-9. PMID:12467703
