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. Author manuscript; available in PMC: 2016 Nov 1.
Published in final edited form as: Trends Genet. 2015 Sep 29;31(11):627–636. doi: 10.1016/j.tig.2015.09.001

Figure 2. Evolutionary conflict at the transferrin-TbpA interface.

Figure 2

A. Co-crystal structure (PDB: 3V8X) of human transferrin bound to TbpA from N. meningitidis. Side-chains of rapidly evolving amino acid positions in primate transferrin are shown in blue, with rapidly evolving TbpA sites among human pathogens shown in red (as described in reference 36). B. Schematic highlighting rapidly evolving regions in primate transferrin. Sites subject to positive selection are denoted with blue arrows; a variable site in humans (the C2 variant) is marked by a white arrow. Divergent amino acids among humans and other primates are shown in blue, and the ability of human-adapted TbpA to recognize each transferrin ortholog is shown at right. The human transferrin C2 variant is recognized by TbpA from some, but not all pathogens.