Implications of an Antiparallel Dimeric Structure of Nonphosphorylated STAT1 for the Activation-Inactivation Cycle

IFN-γ treatment of cells leads to tyrosine phosphorylation of signal transducer and activator of transcription (STAT) 1 followed by dimerization through a reciprocal Src homology 2-phosphotyrosine interaction near the -COOH end of each monomer, forming a parallel structure that accumulates in the nu...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2005-03, Vol.102 (11), p.3966-3971
Hauptverfasser:	Zhong, Minghao, Henriksen, Melissa A., Takeuchi, Kenji, Schaefer, Olaf, Liu, Bin, Hoeve, Johanna ten, Ren, Zhiyong, Mao, Xiang, Chen, Xiaomin, Shuai, Ke, Darnell, James E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies Binding sites Biochemistry Biological Sciences Biomarkers Blotting, Western Crystal structure Dimerization Dimers DNA DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Genetic mutation Humans Immunoprecipitation Molecular interactions Molecules Monomers Mutation Phosphatases Phosphorylation Signal transduction STAT1 Transcription Factor Trans-Activators - genetics Trans-Activators - metabolism
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