MAP kinase phosphorylation-dependent activation of Elk-1 leads to activation of the co-activator p300
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چکیده
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Activation Mechanism of the MAP Kinase ERK2 by Dual Phosphorylation
The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded, bringing the phosphothreonine and phosphotyrosine into alignment with surface arginine-rich binding sites. Conformational changes occur in the lip and neighboring structures, including the P+1 site, the MAP kinase inse...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2003
ISSN: 1460-2075
DOI: 10.1093/emboj/cdg028