Title : DNA binding reduces the dissociation rate of STAT1 dimers and impairs the interdimeric exchange of protomers.

Pub. Date : 2014 Dec 20

PMID : 25526807






2 Functional Relationships(s)
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1 BACKGROUND: A shift between two dimer conformations has been proposed for the transcription factor STAT1 (signal transducer and activator of transcription 1) which links DNA binding of the parallel dimer to tyrosine dephosphorylation of the antiparallel dimer as two consecutive and important steps in interferon- gamma (IFNgamma)-mediated signalling. Tyrosine interferon gamma Homo sapiens
2 BACKGROUND: A shift between two dimer conformations has been proposed for the transcription factor STAT1 (signal transducer and activator of transcription 1) which links DNA binding of the parallel dimer to tyrosine dephosphorylation of the antiparallel dimer as two consecutive and important steps in interferon- gamma (IFNgamma)-mediated signalling. Tyrosine interferon gamma Homo sapiens