Joanne C. Krupa

TL;DR: It is shown that HCGP39 is able to bind chitooligosaccharides with micromolar affinity, and this protein could be a lectin that binds chitin-like oligOSaccharide ligands and possibly plays a role in innate responses to chitinous pathogens, such as fungi and nematodes.

TL;DR: Three-dimensional crystal structures of a mature, inactive mutant of human cathepsin L alone and in complex with a peptide derived from histone H3 are reported and systematic analysis of the impact of posttranslational modifications at hist one H3 on substrate selectivity suggests cathePSin L to be highly accommodating of all modified peptides.

TL;DR: The results show that cathepsins K and L and papain, typically considered to act strictly as endopeptidases, can also display dipeptidyl carboxypeptidase activity against the substrate Abz-FRF(4NO2)A and dipeethidyl aminopePTidaseActivity against FR-MCA.

TL;DR: These studies showed that cathepsin B is optimized to act as an exopeptidase, cleaving dipeptides from protein substrates in a successive manner, because of its relaxed specificity in P2' and its other subsites.

TL;DR: The chagasin-cathepsin L complex structure provides details of how the parasite protein inhibits a host enzyme of possible importance in host defense and aids in the development of synthetic inhibitors for use as potential drugs for the treatment of Chagas disease.