Fig. 5 | Scientific Reports

Fig. 5

From: Evolutionary analysis through structural modeling of FAM222 proteins reveals a novel disordered conserved domain in vertebrates that interacts with NLK

Fig. 5

Identification of the revD motif in the DCD222 region. (A) Prediction of SLiMs within the DCD222 domain of hFAM222A using the ELM server, along with their conservation in hFAM222B, laXP, and haXP. (B and C) Interaction of the revD-motif with the docking groove of NLK, where the surface hydrophobicity is represented using a color scale. (D) Average ipTM values for interactions between hFAM222 proteins, the DCD222 region, and its mutants with 12 additional human MAPKs, including NLK.

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