The structure of mitogen-activated protein kinase p38 at 2.1-angstrom resolution
The structure of mitogen-activated protein kinase p38 at 2.1-angstrom resolution
复制标题
DOI：
10.1073/pnas.94.6.2327
复制
发表时间：
1997-03-18
影响因子：
11.1
通讯作者：
Goldsmith, EJ
中科院分区：
文献类型：
--
作者：
Wang, ZL;Harkins, PC;Goldsmith, EJ
有丝分裂原活化蛋白（MAP）激酶p38的结构已经在2.1埃的R因子为21.0%的情况下被解析，使p38成为迄今为止第二个被解析的低活性MAP激酶。尽管p38在拓扑学上与MAP激酶ERK 2相似，但磷酸化Lip在p38中，MAP激酶（活性位点附近的调节环）采用不同的折叠，肽底物结合位点和ATP结合位点也不同于ERK 2，这些结果解释了为什么MAP激酶对不同的活化酶、底物和抑制剂具有特异性，底物和激活剂相互作用的模型对蛋白激酶级联的进化有影响。
The structure of mitogen-activated protein (MAP) kinase p38 has been solved at 2.1-Angstrom to an R factor of 21.0%, making p38 the second low activity MAP kinase solved to date. Although p38 is topologically similar to the MAP kinase ERK2, the phosphorylation Lip (a regulatory loop near the active site) adopts a different fold in p38, The peptide substrate binding site and the ATP binding site are also different from those of ERK2, The results explain why MAP kinases are specific for different activating enzymes, substrates, and inhibitors, A model presented for substrate and activator interactions has implications for the evolution of protein kinase cascades.