MAP kinase ERK2
The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by
Ras and Raf, has been solved in its dephosphorylated, low activity conformation to a
resolution of 2.3Å. In comaprison to the active conformation of cyclic AMP-dependent
protein kinase the two domains of dephosphorylated ERK2 are farther apart and the peptide
binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated
in the active enzyme. Activation of ERK2 thus is likely to involve both global and local
conformational changes.
Atomic structure of the MAP kinase ERK2 at 2.3Å resolution.
Faming Zhang, Arne Strand, David Robbins, Melanie H Cobb and Elizabeth J.
Goldsmith.
Nature, 367:704-711(1994)