Fig. 2: Sequence-based predictions of DIP/Dpr specificity residues and common binding determinants. | Nature Communications

Fig. 2: Sequence-based predictions of DIP/Dpr specificity residues and common binding determinants.

From: DIP/Dpr interactions and the evolutionary design of specificity in protein families

Fig. 2

a Alignment of sequence logos corresponding to interfacial residues of DIP and Dpr Insecta orthologs. Predictions of specificity determining positions using sequence-based methods (GroupSim, SDPpred, SPEER, and Multi-Harmony) are given below logos in different shades of gray as specified in boxed inset. Bar on the left of logos indicates color of the DIP/Dpr subgroup (Fig. 1b). Family-wide numbering of interfacial positions is given above the alignment. The correspondence between protein specific (UniProt) and family-wide numbering is given in Supplementary Table 1. See Methods section for details on sequence logo preparation. b Common binding determinants of DIP/Dpr dimers depicted on ribbon Ig1–Ig1 interfaces in sticks. Hydrophobic interfacial residues are in yellow. Conserved buried hydrogen bonds are depicted by dotted lines. Interfacial positions enclosed in boxes follow family-wide numbering and are annotated with identities of conserved amino-acids.

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