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. Author manuscript; available in PMC: 2014 Dec 17.
Published in final edited form as: Cell. 2014 Jul 3;158(1):132–142. doi: 10.1016/j.cell.2014.04.048

Figure 1. Unique properties of the DP2 acidic pocket.

Figure 1

(A) Three groups of DP2-binding peptides are listed. The top group are self-peptides that are commonly found bound to DP2 (Díaz et al., 2005), but cannot present Be2+ to AV22. The middle group contains examples from a series of mimotope peptides found in a positional scanning library (Falta et al., 2013) that can present Be2+ to AV22. The bottom group contains examples of self-peptides that can present Be2+ to AV22, identified by their similarity to the mimotope peptides (Falta et al., 2013).

(B) Details of the acidic pocket of DP2 occupied by each of three peptides at the top of (A), pDRa, pA28, pRAS. Ribbons: DP2α cyan; DP2β magenta. Wireframe with CPK coloring: Peptide and side chains of DP2 β26E, β68E, and β69E. Potential H-bond/salt bridges, green lines.

See also Figure S1 and Table S1.