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Fig. 1 | BMC Biochemistry

Fig. 1

From: Identification of inhibitors that target dual-specificity phosphatase 5 provide new insights into the binding requirements for the two phosphate pockets

Fig. 1

DUSP5 and ERK2 Models. a Model depicting the two domains of DUSP5. This model is comprised of two domains, the ERK binding domain (EBD) and phosphatase domain (PD), and illustrates the relative location of the domains and their connection via a 30 amino acid linker of unknown structure. The homology model of EBD was constructed using the solution structure (21 % identity and 35 % homology) of human MKP-3 protein (PDB:1HZM) as a template [35]. The phosphatase domain is the previously reported crystal structure (PDB:2G6Z) [16]. The 30 amino acid linker region connecting the two domains was prepared manually, and is of unknown structure. The S147P mutation present in patients with vascular anomalies is shown in green, and arginine-rich basic regions have been identified. b DUSP5 and ERK2 binding model. DUSP5 (blue) is positioned similarly in respects to panel a with the EBD to the left and PD to the right, wrapping around human ERK2 in yellow. Model was prepared as described in our previous paper [8]. The linker region may have the first 11 amino acids as helical based secondary structure predictions [4648], although this was only found to be loosely helical after molecular dynamics simulations. The ERK2 (yellow) structure (PDB:3I60) [18] is shown between the DUSP5 domains to illustrate relative shape and size complementarity; and, relative orientation of ERK2 and DUSP5 is based on the molecular dynamics simulation and associated analysis presented in our previous paper [8]

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