| Type: | Family | Name: | Mitogen-activated protein (MAP) kinase phosphatase |
| Description: | MAP Kinase Phosphatases (MKPs) are members of the dual specificity phosphatase family [, ]. MKPs constitute a class of phosphatases that reverse the activation of MAP (mitogen activated protein) kinases by dephosphorylating critical tyrosineand threonine residues []. This regulation is mediated via interaction of aKinase Interaction Motif (KIM) with the common docking domain of the kinase - this motif is shared with a number of other protein families that interactwith MAP kinases: these include kinases (MEKs), phosphatases (PTP-SL) and transcription factors (Elk1). MKPs also share an active site motif with theprotein tyrosine phosphatases (PTPs). Different MKPs exhibit specificity towards different members of the MAP kinase family [].The structure of the MPK catalytic domain is similar to that of the PTPs - the fold exhibits a complex mixed alpha-/beta-architecture. Thecatalytic mechanism involves a general acid (Asp92 in 1VHR) and a catalytic cysteine (130 in 1VHR), which acts as a nucleophile. | Short Name: | MKP |
