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. Author manuscript; available in PMC: 2013 Mar 7.
Published in final edited form as: Structure. 2012 Mar 7;20(3):479–486. doi: 10.1016/j.str.2012.01.009

Figure 5. Comparison of VLRB Binding Interfaces with Different Antigens.

Figure 5

The concave surface of each VLRB is represented as a surface highlighting the proximity of each amino acid to its respective antigen in angstroms. The surface used by VLRB to contact antigens favors the use of the C-terminal LRR motifs and VLR4 is heavily biased towards the used of the C-terminal ends of the ß-strands of these motifs. The LRRCT motif (pink) of each VLRB shows dramatically different lengths and conformations in their LRRCT-loops.