E??64c??Hydrazide: A Lead Structure for the Development of Irreversible Cathepsin C Inhibitors

…, M Grundhuber, CP Sommerhoff, N Schaschke

Index: Radzey, Hanna; Rethmeier, Markus; Klimpel, Dennis; Grundhuber, Maresa; Sommerhoff, Christian P.; Schaschke, Norbert ChemMedChem, 2013 , vol. 8, # 8 p. 1314 - 1321

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Abstract

Abstract Cathepsin C is a papain-like cysteine protease with dipeptidyl aminopeptidase activity that is thought to activate various granule-associated serine proteases. Its exopeptidase activity is structurally explained by the so-called exclusion domain, which blocks the active-site cleft beyond the S2 site and, with its Asp 1 residue, provides an anchoring point for the N terminus of peptide and protein substrates. Here, the hydrazide ...