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. Author manuscript; available in PMC: 2015 May 17.
Published in final edited form as: Nat Commun. 2014 Nov 17;5:5475. doi: 10.1038/ncomms6475

Figure 1. Design of photocaged dimerizer cTMP-Htag.

Figure 1

(a) Chemical structure and schematic diagrams of cTMP-Htag 1 and its two receptors: E. coli DHFR (eDHFR) and the Halotag protein (Haloenzyme). (b) Schematic of light-induced protein dimerization in living cells via cTMP-Htag. The cell-permeable photocaged dimerizer enters cells and irreversibly reacts with the Haloenzyme. Any unreacted dimerizer is removed by washout. The photocage prevents binding with eDHFR before illumination, and is removed by irradiation with ~385–405nm light, allowing eDHFR to bind the uncaged TMP group, thus dimerizing eDHFR and Haloenzyme.

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