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Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
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Structural basis for DNA recognition by STAT6.

Jing Li1,2, Jose Pindado Rodriguez3, Fengfeng Niu1

  • 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Proceedings of the National Academy of Sciences of the United States of America
|November 3, 2016
PubMed
Summary
This summary is machine-generated.

Signal transducer and activator of transcription 6 (STAT6) binds DNA via a unique mechanism involving conformational changes. A specific residue, H415, dictates STAT6

Keywords:
JAK-STAT pathwayN4 site DNA recognitionSTAT6antiviral innate immunitycrystal structure

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Area of Science:

  • Molecular biology
  • Structural biology
  • Immunology

Background:

  • STAT6 is crucial for IL-4/IL-13 signaling and innate immunity.
  • STAT6 dysregulation is implicated in asthma, immune disorders, and cancer.
  • Understanding STAT6 DNA binding is key to therapeutic targeting.

Purpose of the Study:

  • To elucidate the molecular mechanism of STAT6 DNA recognition.
  • To determine the structural basis for STAT6's differential binding to N3 and N4 DNA sites.

Main Methods:

  • X-ray crystallography of STAT6 core fragment (STAT6CF) alone and with DNA.
  • Molecular dynamics simulations.
  • Small-angle X-ray scattering (SAXS).
  • Site-directed mutagenesis (H415N).

Main Results:

  • STAT6 undergoes significant conformational changes upon DNA binding.
  • A unique residue, H415, and inter-protomer angle are critical for DNA site discrimination.
  • H415N mutation alters STAT6 affinity for N3 and N4 DNA sites in vitro and in vivo.

Conclusions:

  • The study reveals the structural basis for STAT6 DNA binding specificity.
  • Findings provide insights into STAT family DNA recognition mechanisms.
  • This work supports the development of STAT6-targeted therapies.