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. Author manuscript; available in PMC: 2014 Mar 29.
Published in final edited form as: Curr Opin Struct Biol. 2012 Dec 22;23(1):82–89. doi: 10.1016/j.sbi.2012.11.003

Figure 1.

Figure 1

Post translational modification of human PreProIAPP to form the mature IAPP sequence: (a) The primary sequence of the 89-residue human PreProIAPP. The 22 residue signaling sequence is shown in black, the N-terminal and C-terminal proIAPP flanking regions are shown in blue, and the mature IAPP sequence is shown in red. (b) The primary sequence of the 67-residue human proIAPP. Before secretion, proIAPP is cleaved by the prohormone convertases PC2 and PC(1/3) at two dibasic sites, indicated by arrows. Further processing by the CPE/PAM complex results in an amidated Tyr at the C-terminus of mature IAPP. (c) The mature 37-residue human IAPP. The biologically active peptide has an intramolecular disulfide bridge between Cys-2 and Cys-7 and an amidated C-terminus. Positively charged residues are underlined in the ProIAPP and mature IAPP sequences.