Binding Mechanism Analysis between AhR Protein and Typical Polybrominated Diphenyl Ether via Molecule Docking
- 10.2991/aiea-16.2016.83How to use a DOI?
- Polybrominated diphenyl ethers; aryl hydrocarbon receptor; homology modeling; molecular docking.
In this paper, BDE-85 was selected as the typical polybrominated diphenyl ether (PBDE) because of its obvious biological toxicity and the receptor binding affinity (RBA) was taken as the index of biological toxicity. By using the homology modeling, the aryl hydrocarbon receptor (AhR) protein molecule was established for researching the binding mechanism between the AhR protein and BDE-85. The obtained results showed that: the RSMD value of the established AhR protein was 0.049, present reasonable molecule structure and amino acid sequence; among active residues, the hydrophobic amino form a hydrophobic region to improve the molecule docking between the AhR protein and BDE-85, resulting in significant biological toxicity of BDE-85.
- © 2016, the Authors. Published by Atlantis Press.
- Open Access
- This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).
Cite this article
TY - CONF AU - Long Jiang AU - Gaojun Liu AU - Qing Li PY - 2016/11 DA - 2016/11 TI - Binding Mechanism Analysis between AhR Protein and Typical Polybrominated Diphenyl Ether via Molecule Docking BT - Proceedings of the 2016 International Conference on Artificial Intelligence and Engineering Applications PB - Atlantis Press SP - 464 EP - 467 SN - 2352-538X UR - https://doi.org/10.2991/aiea-16.2016.83 DO - 10.2991/aiea-16.2016.83 ID - Jiang2016/11 ER -