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dc.contributor.authorWang, Z. L.zh_CN
dc.contributor.authorHarkins, P. C.zh_CN
dc.contributor.authorUlevitch, R. J.zh_CN
dc.contributor.authorHan, J. H.zh_CN
dc.contributor.authorCobb, M. H.zh_CN
dc.contributor.authorGoldsmith, E. J.zh_CN
dc.contributor.author韩家淮zh_CN
dc.date.accessioned2013-12-12T02:24:46Z
dc.date.available2013-12-12T02:24:46Z
dc.date.issued1997zh_CN
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America,94(6):2327-2332zh_CN
dc.identifier.issn0027-8424zh_CN
dc.identifier.otherISI:A1997WP33400045zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65891
dc.description.abstractThe 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.zh_CN
dc.language.isoen_USzh_CN
dc.subjectSIGNAL-TRANSDUCTION PATHWAYzh_CN
dc.subjectMAP KINASEzh_CN
dc.subjectCRYSTAL-STRUCTUREzh_CN
dc.subjectCATALYTIC SUBUNITzh_CN
dc.subjectMAMMALIAN-CELLSzh_CN
dc.subjectGROWTH-FACTORzh_CN
dc.subjectC-MYCzh_CN
dc.subjectPHOSPHORYLATIONzh_CN
dc.subjectDOMAINzh_CN
dc.subjectINHIBITORSzh_CN
dc.titleThe structure of mitogen-activated protein kinase p38 at 21-angstrom resolutionzh_CN
dc.typeArticlezh_CN


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