Exploring binding sites other than the catalytic core in the crystal structure of the catalytic domain of MKP-4.

The article discusses a research study on other binding sites in the crystal structure of map kinase phosphatase 4 (MKP-4) catalytic domain. Researchers cloned and subcloned the MKP-4C residues from human kidney that contain maltose-binding protein (MBP), collected the data on crystallization and proceeded with the molecular-replacement method and virtual screening. Results showed that one MKP-4C molecule was in the assymetric unit with no indication of oligometric interaction in the crystal.