Structural Basis for Sequence Specific DNA Binding and Protein Dimerization of HOXA13
2011
Structure of HOXA13 Dimer Bound to DNA
publication
Evidence: high
Author Information
Author(s): Zhang Yonghong, Larsen Christine A., Stadler H. Scott, Ames James B.
Primary Institution: Department of Chemistry, University of California Davis
Hypothesis
How does HOXA13 mediate tissue-specific expression of its target genes?
Conclusion
HOXA13 dimerization is required to activate transcription of target genes.
Supporting Evidence
- HOXA13 binds tightly to specific DNA targets without the aid of cofactors.
- Mutations in HOXA13 are linked to developmental disorders.
- The N-terminal arm of HOXA13 makes important contacts in the DNA minor groove.
- Hydrophobic contacts between HOXA13 and DNA are crucial for sequence recognition.
- HOXA13 dimerization enhances its ability to regulate gene expression.
Takeaway
This study shows that a protein called HOXA13 can stick to DNA in a special way, and it needs to form pairs to help control how genes work.
Methodology
NMR spectroscopy was used to determine the structure of the HOXA13 dimer bound to DNA.
Digital Object Identifier (DOI)
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