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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-80BA-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-80C0-A
Genre: Journal Article

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Russo, L.1, Author              
Giller, K.1, Author              
Pfitzner, E., Author
Griesinger, C.1, Author              
Becker, S.1, Author              
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1Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 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.

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Language(s): eng - English
 Dates: 2017-12-04
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41598-017-17088-5
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Title: Scientific Reports
Source Genre: Journal
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Pages: 12 Volume / Issue: 7 Sequence Number: 16845 Start / End Page: - Identifier: -