2gph
|
Docking motif interactions in the MAP kinase ERK2
OverviewOverview
MAP kinases bind activating kinases, phosphatases, and substrates through, docking interactions. Here, we report a 1.9 A crystallographic analysis of, inactive ERK2 bound to a "D motif" docking peptide (pepHePTP) derived from, hematopoietic tyrosine phosphatase, a negative regulator of ERK2. In this, complex, the complete D motif interaction defined by mutagenic analysis is, observed, including extensive electrostatic interactions with the "CD", site of the kinase. Large conformational changes occur in the activation, loop where the dual phosphorylation sites, which are buried in the, inactive form of ERK2, become exposed to solvent in the complex. Similar, conformational changes occur in a complex between ERK2 and a MEK2 (MAP/ERK, kinase-2)-derived D motif peptide (pepMEK2). D motif peptides are known to, bind homologous loci in the MAP kinases p38alpha and JNK1, also inducing, conformational changes in these enzymes. However, the binding interactions, and conformational changes are unique to each, thus contributing to, specificity among MAP kinases.
About this StructureAbout this Structure
2GPH is a Protein complex structure of sequences from Rattus norvegicus. Active as Mitogen-activated protein kinase, with EC number 2.7.11.24 Full crystallographic information is available from OCA.
ReferenceReference
Docking interactions induce exposure of activation loop in the MAP kinase ERK2., Zhou T, Sun L, Humphreys J, Goldsmith EJ, Structure. 2006 Jun;14(6):1011-9. PMID:16765894
Page seeded by OCA on Mon Nov 12 22:20:45 2007