Back

Structural insights into viral hijacking of p53 by E6 and E6AP

Sandate, C. R.; Chakraborty, D.; Kater, L.; Kempf, G.; Thoma, N. H.

2023-11-02 biophysics
10.1101/2023.11.01.565136 bioRxiv
Show abstract

The E3-ubiquitin ligase E6AP degrades p53 when complexed with the viral protein E6 from human papilloma virus (HPV), which contributes to the transformation of cells in HPV-related cancers. Previous crystal structures of the E6AP-E6-p53 ternary complex have implicated a peptide containing an LxxLL motif from E6AP as the interface between the three proteins. However, the contributions to the ternary complex from the remainder of the E6AP protein remain unknown. We reexamined this complex using cryo-EM and full-length proteins and find additional protein interaction interfaces involving a previously uncharacterized domain of E6AP. Additionally, we observe that the ternary complex forms both 1:1:1 and 2:2:2 stochiometric complexes comprised of E6AP, E6 and p53.

Matching journals

The top 3 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.