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Allosteric Database


NAR Molecular Biology Database Collection entry number 1396
Huang, Zhimin; Mou, Linkai; Shen, Qiancheng; Lu, Shaoyong; Liu, Xinyi; Wang, Guanqiao; Li, Shuai; Geng, Lv; Chen, Guoqiang; Zhang, Jian

Database Description

Allostery is the most direct and efficient way for regulation of biological macromolecule function induced by the binding of a ligand at an allosteric site topographically distinct from the orthosteric site. Due to the inherent high receptor selectivity and lower target-based toxicity, allosteric regulation is also expected to play a more positive role in drug discovery and bioengineering, leading to rapid growth on allosteric findings. Allosteric Database (ASD) provides a central resource for the display, search and analysis of the structure, function and related annotation for allosteric molecules. Currently, ASD contains allosteric proteins from more than 100 species and modulators in three categories(activators, inhibitors, and regulators). Each protein is annotated with detailed description of allostery, biological process and related diseases, and each modulator with binding affinity, physicochemical properties and therapeutic area. Integrating the information of allosteric proteins in ASD should allow for the prediction of allostery for unknown proteins and eventually make them ideal targets for experimental validation. In addition, modulators curated in ASD can be used to investigate potent allosteric targets for the query compound, and also help chemists to implement structure modifications for novel allosteric drug design. Therefore, ASD could be a platform and a starting point for biologists and medicinal chemists for furthering allosteric research.

Recent Developments

Recently, ASD in 2012 has doubly expanded allosteric proteins, allosteric diseases and allosteric modulators. Experimentally validated allosteric pathway, structural pairs of orthosteric and allosteric sites, and allosteric DNAs and RNAs were added. Furthermore, a suite of computational modules to help allosteric studies were added in 2012.

Acknowledgements

We thank all staff of MDL at Shanghai Jiaotong University School of Medicine for the data curation, annotation, release and web development.

References

1. Changeux JP. Allostery and the monod-wyman-changeux model after 50 years. Annu Rev Biophys. 2012,41:103-133.
2. Weinkam P, Pons J, Sali A. Structure-based model of allostery predicts coupling between distant sitesProc Natl Acad Sci U S A. 2012,109(13):4875-4880.
3. Vinkenborg JL, Karnowski N, Famulok M. Aptamers for allosteric regulation. Nat Chem Biol. 2011,7(8):519-527.
4. Reynolds KA, McLaughlin RN, Ranganathan R. Hot spots for allosteric regulation on protein surfaces. Cell. 2011,147(7):1564-1575.
5. Changeux JP. Allosteric Receptors From Electric Organ to Cognition. Annu Rev Pharmacol Toxicol. 2010 50:1-38.
6. Kenakin TP. Ligand Dection in the Allosteric World. J Biomol Screen. 2010 15(2):119-130.


Go to the abstract in the NAR 2014 Database Issue.
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