Tuesday, February 26, 2008

The current issue of Chemistry & Biology features an article, highlighted on the journal cover, reporting the design and synthesis of a small molecule that activates protein phophatase-1 (PP-1). The activity of PP-1 is normally controlled by a wide variety of binding proteins, each containing a consensus sequence (RVXF) recognized by a regulatory site on PP-1. Tappan and Chamberlin (pp. 167-174) demonstrate that a small molecule mimic of this regulatory consensus sequence activates PP-1 in two ways, despite the fact that its structure is, paradoxically, an analog of the well-known microcystin family of potent inhibitors.

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