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Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain
We report experiments that infer a radical reorientation of tyrosine-phosphorylated parallel STAT1 dimers to an antiparallel form. Such a change in structure allows easy access to a phosphatase. With differentially epitope-tagged molecules, we show that the two monomers of a dimer remain together du...
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| Main Authors: | , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
Cold Spring Harbor Laboratory Press
2006
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1698445/ https://ncbi.nlm.nih.gov/pubmed/17182865 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.1485406 |
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