Fig. 1: Tryptophan mutation at residue 435 confers structural and dynamic changes to the MKP5 allosteric pocket.
From: Dynamic and structural insights into allosteric regulation on MKP5 a dual-specificity phosphatase
a Left to right, structural overlay of the catalytic domain of WT MKP5 (light gray) and Y435W (marine blue), WT MKP5 (light gray) and Cmpd 1-bound Y435W (light blue), Y435W (marine blue) and Cmpd 1-bound Y435W (light blue) and WT-Cmpd-1 bound (dark gray) overlayed with Y435W-Cmpd-1 bound (light blue). The structural differences in the α4-α5 loop and the catalytic pocket are labeled. b Network of hydrogen bonds that connects α4-α5 loop of the allosteric pocket to the catalytic pocket in the apo WT MKP5 (left), and the dynamic changes in the secondary structure and new hydrogen bonds formed upon Cmpd 1 binding to WT MKP5 (middle) and to Y435W MKP5 (right).
