Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.

Comparing this with the archetypal C1A cysteine proteases, the loop does not appear to exhibit any conformational change that is likely to be significant upon propeptide cleavage in papain (Kamphuis et al. , 1984 ▶ ; Roy et al. , 2012 ▶ ), cathepsin L (Adams-Cioaba et al. , 2011 ▶ ; Coulombe et al. , 1996 ▶ ) or cathepsin B (Musil et al. , 1991 ▶ ; Podobnik et al. , 1997 ▶ ; Turk et al. , 1996 ▶ ).

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