PROJECTS

We study protein phosphatase 5 (PP5), a Ser/Thr phosphatase with a unique N-terminal domain consisting of 3 tetratricopeptide repeats (TPRs), which binds other proteins and, together with the C-terminal region, inhibits activity. Projects include defining the structural basis for controlling PP5 activity, learning how this enzyme is regulated in cells, and identifying physiological substrates.

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