Figure: HIV1-Vpr inhibition of UNG2 via DDB1/CUL4A (Human-Lentivrus)¶
This figure depicts the mechanism by which HIV1-Vpr inhibits UNG2 via the DDB1/CUL4A ubiquitin ligase pathway. The viral protein Vpr (red circle) acts as a molecular adaptor that binds to DCAF1 (blue rectangle), a substrate adaptor protein. DCAF1 interacts with DDB1, which binds to CUL4A, forming a CRL4-DCAF1-Vpr E3 ubiquitin ligase complex with RBX1. This complex targets UNG2 (green circle), a uracil DNA glycosylase enzyme, for ubiquitination (orange Ub tag) and subsequent degradation. This leads to the inhibition of DNA repair, specifically disrupting base-excision repair and AP site formation via deaminated base removal. The entire process occurs within the nucleus of the host cell, representing a viral strategy to inhibit host DNA repair mechanisms.
Feedback from AI on figure:
{"feedback":"The diagram effectively illustrates the pathway showing how HIV1-Vpr protein inhibits UNG2 through the DDB1/CUL4A complex. The visual presentation is clear and scientifically accurate, with appropriate use of shapes, colors, and labels to distinguish between different proteins and their interactions. The addition of functional annotations for each protein helps viewers understand the specific roles of each component in the pathway. The CRL4-DCAF1-Vpr complex is clearly labeled, and the ubiquitination process leading to DNA repair inhibition is well-represented. The legend provides necessary context without overwhelming the viewer, making this suitable for publication in a high-impact scientific journal.","necessary_changes":null,"optional_changes":null}