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Structural Insight into Anaphase Promoting Complex 3 Structure and Docking with a Natural Inhibitory Compound
Hamzeh Rahimi1, Mohammad Ali Shokrgozar2, Armin Madadkar-Sobhani3
1Department of Molecular Medicine, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Advanced Biomedical Research
|April 13, 2017
Summary
Researchers modeled the APC3 subunit, revealing its superhelical TPR domain structure. They identified a binding pocket for a natural APC inhibitor, aiding anti-cancer drug design targeting the anaphase-promoting complex (APC).
Area of Science:
- Biochemistry
- Structural Biology
- Cell Biology
Background:
- The anaphase-promoting complex (APC) is a crucial Cullin-RING E3 ligase regulating cell cycle control.
- APC targets include anti-cancer agents due to its role in chromosome separation and mitotic exit.
- The APC3 subunit is key for identifying APC activators Cdh1 and Cdc20.
Purpose of the Study:
- To computationally model the structure of the APC3 subunit.
- To investigate the binding of a natural inhibitory compound to APC3.
Main Methods:
- Computational techniques were employed to develop the structural model of APC3.
- The interaction between APC3 and a natural inhibitory compound was analyzed.
Main Results:
- The APC3 structure exhibits numerous anti-parallel helices, forming a superhelical arrangement of tetratrico-peptide repeat (TPR) domains.
- A specific binding pocket for a natural APC3 inhibitor was identified.
Conclusions:
- The study provides insights into the mechanism of APC activation.
- Findings facilitate the design of novel APC inhibitory compounds for therapeutic applications.