5NWX

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

5NWX の概要

• エントリーDOI: 10.2210/pdb5nwx/pdb
• 関連するPDBエントリー: 5NWM
• 分子名称: Nuclear receptor coactivator 1, Signal transducer and activator of transcription 6 (3 entities in total)
• 機能のキーワード: ncoa1, stat6, pas-b domain, transactivation domain, transcription
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Nucleus : P70365; Cytoplasm: P42226
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18264.61

構造登録者

Russo, L.,Giller, K.,Pfitzner, E.,Griesinger, C.,Becker, S. (登録日: 2017-05-08, 公開日: 2017-12-13, 最終更新日: 2024-01-17)

主引用文献

Russo, L.,Giller, K.,Pfitzner, E.,Griesinger, C.,Becker, S.
Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6.
Sci Rep, 7:16845-16845, 2017

PubMed 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/ Leu-Gly-STAT6 complex, the mechanistic details of this interaction are still poorly understood. Here, we determine the structure of the NCoA1/STAT6 complex using Nuclear Magnetic Resonance (NMR) and X-ray crystallography. The STAT6 peptide binds with additional N-terminal amino acids to NCoA1, compared to the STAT6 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.

PubMed: 29203888
DOI: 10.1038/s41598-017-17088-5

実験手法

X-RAY DIFFRACTION (2.51 Å)