Structural modeling reveals a unique interface between TAX1BP1 and NBR1. (A) HEK293T cells were co-transfected with full-length (FL) myc-TAX1BP1 and indicated BFP-V5-NBR1^FL variants. Extracts derived from transfected cells were immunoprecipitated (IP) with protein G dynabeads conjugated with anti-V5 antibody. Input and eluates were resolved by SDS-PAGE followed by immunoblotting (IB) with the indicated antibodies. (B) Predictive structural model of NBR1^725–749 with a dimer TAX1BP1^CC2. The model was generated using AlphaFold AF2-multimer with MMseqs2 through Google Colab. The TIR inset highlights the hydrophobic binding pocket occupied by NBR1^F740 and the backbone interactions mediated by TAX1BP1^R441. The LIR inset highlights the lack of meaningful interactions between NBR1^LIR and TAX1BP1^CC2. (C) Predicted IDDT per position (pLDDT) for NBR1^725–749 as an estimation of model confidence. Blue is high confidence, orange is low confidence. (D) HEK293T cells were co-transfected with full-length (FL) myc-NBR1 and indicated BFP-V5-TAX1BP1 variants. Extracts derived from transfected cells were immunoprecipitated (IP) with protein G dynabeads conjugated with anti-V5 antibody. Input and eluates were resolved by SDS-PAGE followed by immunoblotting (IB) with the indicated antibodies. Source data are available for this figure: SourceData F5.