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Journal Article

Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6.

MPS-Authors
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Russo,  L.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Giller,  K.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.       
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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2508701.pdf
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Supplementary Material (public)

2508701_Suppl.pdf
(Supplementary material), 4MB

Citation

Russo, L., Giller, K., Pfitzner, E., Griesinger, C., & Becker, S. (2017). Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. Scientific Reports, 7: 16845. doi:10.1038/s41598-017-17088-5.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-80BA-9
Abstract
Crucial for immune and anti-inflammatory cellular responses, signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 and -13 -induced tyrosine phosphorylation by direct interaction with coactivators. The interaction of STAT6 with nuclear coactivator 1 (NCoA1) is mediated by a short region of the STAT6 transactivation domain that includes the motif LXXLL and interacts with the PAS-B domain of NCoA1. Despite the availability of an X-ray structure of the PAS-B domain/ Leu794-Gly814-STAT6 complex, the mechanistic details of this interaction are still poorly understood. Here, we determine the structure of the NCoA1257-385/STAT6783-814 complex using Nuclear Magnetic Resonance (NMR) and X-ray crystallography. The STAT6783-814 peptide binds with additional N-terminal amino acids to NCoA1257-385, compared to the STAT6794-814 peptide, explaining its higher affinity. Secondary and tertiary structures existing in the free peptide are more highly populated in the complex, suggesting binding by conformational selection.