view article

Figure 3
Structural alignment of murine hybridoma 15C4 homology models and the MagaFab crystal structure. (a) All residues interacting with the peptide and its surroundings are conserved. MagaFab is shown in orange. Murine 15C4 heavy and light variable domains are shown in green and blue, respectively. (b) The same as in (a) but rotated by 90°. (c) Potential flexibility of the VH loop. Murine 15C4 variable heavy domain (VH, green) shows a different conformation of the VH loop compared with the same loop in MagaFab (orange) that partially stabilizes the peptide. While the MagaFab variable light domain (VL, orange) contains a leucine at position 50, the murine homologue (blue) features a phenylalanine. These observations together could point to an important mutation location since the residue at position 50 could interact with the loop and alter its conformation, therefore modifying the affinity of MagaFab for the peptide and possibly for LRG1.

Journal logoSTRUCTURAL
ISSN: 2059-7983
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds