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. 2019 Jul 20;11(7):425. doi: 10.3390/toxins11070425

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Representative structures of the precursors of (A) scorpion (C. noxius) bifunctional PAM and mono-functional PHMm and PALm; (B) mammalian (R. norvegicus) PAM-1 and PAM-2 isoforms; (C) monofunctional PHMm, PAL1m and PAL2m in D. melanogaster. Structural and sequence features are indicated as: SP, Signal peptide; PP, Propeptide; MSD, Membrane Spanning Domain; CD, Cytosolic Domain; KK, RK, KR and RR, putative proprotein convertase cleavage sites at basic dyads; G, predicted glycosylation site; PHMcc, catalytic core of the PHM domain.