2GPH
Docking motif interactions in the MAP kinase ERK2
Summary for 2GPH
| Entry DOI | 10.2210/pdb2gph/pdb |
| Descriptor | Mitogen-activated protein kinase 1, Tyrosine-protein phosphatase non-receptor type 7 (3 entities in total) |
| Functional Keywords | erk2, docking interaction, d-motif, allostery, cd-site, phosphatase-derived peptide, processing conformation, transferase |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cytoplasm, cytoskeleton, spindle : P63086 Cytoplasm : P35236 |
| Total number of polymer chains | 2 |
| Total formula weight | 44025.65 |
| Authors | Zhou, T.,Sun, L.,Humphreys, J.,Goldsmith, E.J. (deposition date: 2006-04-17, release date: 2006-07-04, Last modification date: 2024-11-06) |
| Primary citation | Zhou, T.,Sun, L.,Humphreys, J.,Goldsmith, E.J. Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2. Structure, 14:1011-1019, 2006 Cited by PubMed Abstract: 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. PubMed: 16765894DOI: 10.1016/j.str.2006.04.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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