Location of the epitopes for mAbs 9C9 and 6G6.

<p>(A) Same view as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0108235#pone-0108235-g006" target="_blank">Figure 6A &amp; C</a>. The epitope regions for mAb 9C9 are shown: residues 283–297 (colored brown), residues 224–227 (from the 223–242 peptide, colored dark green) and residues 320–322 (from the 308–322 peptide, colored magenta). (B) A +180<sup>o</sup> rotation about the Y-axis from view shown in panel (A), showing the non-catalytic face of HtrA3. Residues 228–242 are colored dark green and 308–319 are colored magenta. (C) The epitope regions for mAb 6G6 are shown: residues 73–78 (from the 73–92 peptide, colored dark grey), residues 288–302 (colored blue), residues 322–327 (from the 313–327 peptide, colored purple), and residues 398–412 (colored orange). (D) A +180<sup>o</sup> rotation about the Y-axis from view shown in panel (C), showing the non-catalytic face of HtrA3. Residues 79–92 are colored dark grey and 313–321 are colored purple. The 6G6 epitope residues 133–147 (colored white) are now visible on the protease domain surface. (E) Close up view of panel (D) showing the 6G6 epitope regions on the non-catalytic face of HtrA3. Distances between some of the epitope regions are shown in Å. The arrow indicates the direction the PDZ domain would need to move to place the 6G6 epitope residues 398–412 (colored orange) in closer to the residues 313–321 (colored purple), 133–147 (colored white) and 79–92 (colored dark grey). In panels (A) and (C), the location of the catalytic site in each monomer is indicated by a yellow asterix.</p>