Structural Insight into Anaphase Promoting Complex 3 Structure and Docking with a Natural Inhibitory Compound

Anaphase promoting complex (APC) is the biggest Cullin‑RING E3 ligase and is very important in cell cycle control; many anti‑cancer agents target this. APC controls the onset of chromosome separation and mitotic exit through securin and cyclin B degradation, respectively. Its APC3 subunit identifies the APC activators‑Cdh1 and Cdc20.

The structural model of the APC3 subunit of APC was developed by means of computational techniques; the binding of a natural inhibitory compound to APC3 was also investigated.

It was found that APC3 structure consists of numerous helices organized in anti‑parallel and the overall model is superhelical of tetratrico‑peptide repeat (TPR) domains. Furthermore, binding pocket of the natural inhibitory compound as APC3 inhibitor was shown.

The findings are beneficial to understand the mechanism of the APC activation and design inhibitory compounds