The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the在活性酶中磷酸化的两个残基 。因此 ，ERK2的激活可能涉及全球和局部构象变化 。
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文章不错《MAP激酶ERK2的原子结构在2.3Å分辨率下》内容很有帮助