The structure of mitogen-activated protein kinase p38 at 21-angstrom resolution | |
Wang, Z. L. ; Harkins, P. C. ; Ulevitch, R. J. ; Han, J. H. ; Cobb, M. H. ; Goldsmith, E. J. ; Han JH(韩家淮) | |
1997 | |
关键词 | SIGNAL-TRANSDUCTION PATHWAY MAP KINASE CRYSTAL-STRUCTURE CATALYTIC SUBUNIT MAMMALIAN-CELLS GROWTH-FACTOR C-MYC PHOSPHORYLATION DOMAIN INHIBITORS |
英文摘要 | 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. |
语种 | 英语 |
内容类型 | 期刊论文 |
源URL | [http://dspace.xmu.edu.cn/handle/2288/65891] ![]() |
专题 | 生命科学-已发表论文 |
推荐引用方式 GB/T 7714 | Wang, Z. L.,Harkins, P. C.,Ulevitch, R. J.,et al. The structure of mitogen-activated protein kinase p38 at 21-angstrom resolution[J],1997. |
APA | Wang, Z. L..,Harkins, P. C..,Ulevitch, R. J..,Han, J. H..,Cobb, M. H..,...&韩家淮.(1997).The structure of mitogen-activated protein kinase p38 at 21-angstrom resolution.. |
MLA | Wang, Z. L.,et al."The structure of mitogen-activated protein kinase p38 at 21-angstrom resolution".(1997). |
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