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. Author manuscript; available in PMC: 2020 Dec 9.
Published in final edited form as: Bioconjug Chem. 2015 Jun 3;26(6):1120–1128. doi: 10.1021/acs.bioconjchem.5b00190

Figure 1. HA22-LR.

Figure 1.

A. A hypothetical cartoon model structure of the PE-based RIT HA22-LR is shown. The Fv is colored blue, with cystines represented in orange. The catalytic fragment of PE is colored red, and the furin cleavage site is yellow. Residues 607–613 of native PE are disordered in the crystal structure and are not shown here. B. The furin cleavage site of HA22-LR is shown. The position and identity of amino acid residues at the native furin cleavage site of PE are shown. Residue numbering is based on the 613-residue native PE. Protease substrate position is based on standard Schechter and Berger nomenclature. Point mutations at the PE furin cleavage site, hypothesized to create a more efficient substrate for furin hydrolysis, are indicated.