Skip to main content
. 2014 Oct 28;29(1):70–80. doi: 10.1096/fj.14-252262

Figure 5.

Figure 5.

The 537-10D and KD-247 target the same IGPGR epitope using different modes of V3 binding. (A) 537-10D Fab (heavy and light chains in dark and light gray) in complex with an MN V3 peptide (yellow, PDB ID: 3GHE). The primary binding interactions occur in the CDR H3 loop (purple). (B) KD-247 Fab bound to the RP142 V3 peptide (same colors as in (A)). Most of the binding interactions occur in the CDR L1 loop (cyan). (C) Sequence alignment of the KD-247 and 537-10D variable regions (CDR regions in red). Identical residues are highlighted in blue and similar residues in yellow. Asterisks mark the residues making interactions with Arg315 of the RP142 V3 peptide. Sequence alignment was performed by the Sequence Manipulation Suite (http://www.bioinformatics.org/sms2/index.html). CDRs were labeled on the basis of previously published sequences (27, 59).