Figure 1

Sequence and structure of JO-1. Panel (a) shows the amino acid sequence of JO-1 with the 6× His-tag highlighted in grey, the dimerization domain is shown in bold text and highlighted in light blue, and the Ad3 knob highlighted in yellow. The affinity-enhancing V239D mutation and two internal cysteines at aa80 and aa255 are indicated above their respective residue. The H-I loop is underlined. In dimerization domain-deleted mutants, residues deleted are shown by the dashed box. Cysteinyl residues were inserted at locations shown by black arrows in each GB protein indicated next to the arrow. Panel (b) represents side view of the JO-4 trimer structure indicating the location of the N- and C-termini. Panel (c) shows a top down view of the trimer with red arrows highlighting the DSG2 binding loop in this view. The grey shaded oval approximates one JO-1 monomer. The structures are adapted from that of PDB Accession # 1H7Z_A as reported previously^11,12.