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. 2023 Jan 11;24(2):1414. doi: 10.3390/ijms24021414

Figure 3.

Figure 3

The SH3AGS recognition to their targets with the high-affinity binding. (A) Sequence alignment of the SH3 domains of ASAP, GRAF and SKAP proteins showing their identical Cxx(D/E) sequence in RT-loop. The unique cystine and negatively charged residue are labeled by green circles and asterisks. (B) Sequence alignment of the PRM-containing proteins targeted by ASAP, GRAF and SKAP proteins indicating an atypical class-II PRM motif. The unique positively charged residue is highlighted in orange and labeled by orange asterisk. (C) ITC-based affinity measurements of between the SH3AGS domains and their PRMPx+P targets.