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	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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