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. Author manuscript; available in PMC: 2014 Jun 3.
Published in final edited form as: Nat Struct Mol Biol. 2009 Sep 20;16(10):1101–1108. doi: 10.1038/nsmb.1668

Figure 5.

Figure 5

Secondary structure preferences of human caspase-3 and GluC. WebLogo representations of secondary structures from protease cleavage-sites with the scissile bond indicated by the grey arrow. Secondary structure assignments were determined from (a,c) protein structures residing in the PDB as defined by DSSP, or (b,d) predicted by the PSIPRED algorithm. Both human caspase-3 and GluC cleaved substrates in loops as well as helices, but almost never in strands. The intolerance of human caspase-3 for β-strands appears to be restricted around the scissile bond. However, the strand intolerance for GluC is shifted toward the substrates N-terminus. Secondary structure assignments are as follows: L = loop, A = α-helix, B = β-strand.