Zhang F, Strand A, Robbins D, Cobb M H, Goldsmith E J
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas.
Nature. 1994 Feb 24;367(6465):704-11. doi: 10.1038/367704a0.
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 two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.
丝裂原活化蛋白激酶ERK2是一种普遍存在的蛋白激酶，是Ras和Raf调节的靶点，其未磷酸化的低活性构象已被解析，分辨率为2.3埃。未磷酸化的ERK2的两个结构域比环磷酸腺苷依赖性蛋白激酶的活性构象相距更远，并且肽结合位点被酪氨酸185阻断，酪氨酸185是活性酶中被磷酸化的两个残基之一。因此，ERK2的激活可能涉及全局和局部构象变化。
