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. Author manuscript; available in PMC: 2018 Oct 17.
Published in final edited form as: Pharmacol Ther. 2018 Jun 5;190:128–138. doi: 10.1016/j.pharmthera.2018.05.014

Fig. 4.

Fig. 4.

Structure of PRL-CNNM complex. A) Crystal structure of PRL-2 in complex with the CNNM3 CBS-pair domain (Protein Data Bank code 5K22) reveals a tetramer, where CNNM3 forms a dimer and binds to a PRL-2 protein at each side of the dimer. The interaction happens between the extended loop of CNNM3 and active site of PRL-2.B) Crystal structure of PRL-1-CNNM2 (Protein Data Bank code 5MMZ) and C) PRL-3-CNNM3 complex (Protein Data Bank code 5TSR) show similar interaction. D) and E) Comparison of PRL-1 active site conformation in the complex with CNNM2 with the conformation binding to a sulfate group that resemble its phosphate reveals similar conformation re-arrangement.