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Updated: Jan 29, 2026

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling
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Structural basis for DNA recognition by FOXC2

Xiaojuan Chen1,2, Hudie Wei1, Jun Li1

  • 1NHC Key Laboratory of Cancer Proteomics and Laboratory of Structural Biology, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.

Nucleic Acids Research
|February 6, 2019
PubMed

Insights

The FOXC2 transcription factor

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • FOXC1 and FOXC2 are transcription factors crucial for development.
  • FOXC protein mutations are linked to genetic disorders and cancer.

Purpose of the Study:

  • To elucidate the DNA-binding mechanism of human FOXC2.
  • To provide structural insights into FOXC protein-DNA interactions.
  • To understand disease-causing mutations in FOXC1 and FOXC2.

Main Methods:

  • X-ray crystallography to determine protein-DNA complex structures.
  • Biochemical assays to validate binding interactions.
  • Bioinformatics analysis to refine DNA recognition models.

Main Results:

  • Determined two crystal structures of the FOXC2 DNA-binding domain (DBD) bound to DNA.
  • Identified helix H3 as key for base-specific contacts and other regions for phosphate interactions.
  • Revised the DNA recognition mechanism for FOXC proteins.

Conclusions:

  • Established a detailed molecular model for FOXC protein-DNA binding.
  • Provided a structural basis for understanding FOXC1 and FOXC2 related diseases.
  • Advanced the understanding of transcription factor-DNA interactions.

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