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. 2001 Nov 21;70(1):20–25. doi: 10.1086/338456

Figure 3.

Figure 3

Position of mutations (red arrows), in relation to proenteropeptidase exon organization, domains, and amino acid residues forming the active site of the serine protease domain (H825, D876, and S971 [blue arrows]). All four mutations identified are null mutations predicting the absence of a correctly formed active site. The previously described modular structure of proenteropeptidase domains, based on primary-structure comparison, correlates with exon boundaries. SA = signal/anchor sequence; LDLR = LDL receptor–like domain; Muc = mucin-domain; Meprin = meprin-like domain; C1r/s = complement component C1r-like domain; MSCR = macrophage scavenger receptor–like domain.