August 1, 2012 (Vol. 32, No. 14)

URL:
http://mdl.shsmu.edu.cn/ASD/module/mainpage/mainpage.jsp

Rating:
Strong Points: Multiple search/browse options
Weak Points: News section outdated

Summary:

Proteins are subject to modulation by ligands that bind to sites other than the protein’s active site. Many of these so-called allosteric modulators, as well as their protein targets, are catalogued in the Allosteric Database at Shanghai Jiao Tong University. The database contains approximately 8,000 modulator entries, and can be browsed by modulator, target, or index. The modulator browse page is nice in that it provides the 2D structure of each modulator and also denotes whether the modulator is an activator/inhibitor, endogenous, and “druggable”. One annoying limitation to the page is that the actual names of the modulators are not displayed. For that, one must proceed to the pages for individual compounds. There is also the option to search the database, if users have specific compounds/proteins in mind.

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