Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations

The activation/inactivation cycle of STAT transcription factors entails their transition between different dimer conformations. Unphosphorylated STATs can dimerize in an antiparallel conformation via extended interfaces of the globular N-domains, whereas STAT activation triggers a parallel dimer con...

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Détails bibliographiques
Auteurs principaux: Wenta, Nikola, Strauss, Holger, Meyer, Stefanie, Vinkemeier, Uwe
Format: Artigo
Langue:Inglês
Publié: National Academy of Sciences 2008
Sujets:
Biological Sciences
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2453697/
https://ncbi.nlm.nih.gov/pubmed/18591661
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0802130105
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