Fig. 4 | Scientific Reports

Fig. 4

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

Fig. 4

Interaction of the DCD222 region with protein partners. (A) Experimentally validated protein-protein interactions of hFAM222A and hFAM222B retrieved from the STRING database. (B and C) Average ipTM values for protein-protein interactions predicted using AlphaFold3. Values between 0.6 and 0.8 (gray zone) indicate moderate confidence with some uncertainty in binding affinity, while values above 0.8 suggest a highly confident interaction prediction. (D and F) Structural alignment of the DCD222 region of hFAM222A, hFAM222B, laXP, and haXP in complex with the kinase domain of NLK (RMSD=0.570±0.047 Å), colored according to their pLDDT scores. (E) Representative PAE plot of the full-length interaction of hFAM222A with hNLK. Values close to 0 Å indicate high confidence in the spatial relationship between residues or domains. Red dashed boxes highlight the DCD222 region.

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