ArticlePloS one2011
Structural basis for sequence specific DNA binding and protein dimerization of HOXA13.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- METTL1-mediated m7G modification regulates hair follicle cycle via the HOXC13/FOXN1/DSG4 axis.PLoS genetics · 2026Article
- NMR investigation of FOXO4-DNA interaction for discriminating target and non-target DNA sequences.Communications biology · 2024Article
- Structural characterization of PHOX2B and its DNA interaction shed light on the molecular basis of the +7Ala variant pathogenicity in CCHS.Chemical science · 2024Article
- Zinc-chelating postsynaptic density-95 N-terminus impairs its palmitoyl modification.Protein science : a publication of the Protein Society · 2021Article
- Structure of the unique tetrameric STENOFOLIA homeodomain bound with target promoter DNA.Acta crystallographica. Section D, Structural biology · 2021Article
- PRRX1 isoforms cooperate with FOXM1 to regulate the DNA damage response in pancreatic cancer cells.Oncogene · 2019Article
- Two distinct DNA sequences recognized by transcription factors represent enthalpy and entropy optima.eLife · 2018Article
- Structural basis for genome wide recognition of 5-bp GC motifs by SMAD transcription factors.Nature communications · 2017Article
- A missense mutation of HOXA13 underlies hand-foot-genital syndrome in a Chinese family.Journal of genetics · 2017Article
- How proteins bind to DNA: target discrimination and dynamic sequence search by the telomeric protein TRF1.Nucleic acids research · 2017Article
- Impact of cytosine methylation on DNA binding specificities of human transcription factors.Science (New York, N.Y.) · 2017Article
- A novel mutation in homeobox DNA binding domain of HOXC13 gene underlies pure hair and nail ectodermal dysplasia (ECTD9) in a Pakistani family.BMC medical genetics · 2017Article
- Calmodulin Lobes Facilitate Dimerization and Activation of Estrogen Receptor-α.The Journal of biological chemistry · 2017Article
- Genome-Wide Binding of Posterior HOXA/D Transcription Factors Reveals Subgrouping and Association with CTCF.PLoS genetics · 2017Article
- Chemical shift assignments of mouse HOXD13 DNA binding domain bound to duplex DNA.Biomolecular NMR assignments · 2015Article
- HOXB13 and ALX4 induce SLUG expression for the promotion of EMT and cell invasion in ovarian cancer cells.Oncotarget · 2015Article
- Isl1 and Pou4f2 form a complex to regulate target genes in developing retinal ganglion cells.PloS one · 2014Article
- Roles for major histocompatibility complex glycosylation in immune function.Seminars in immunopathology · 2012Review
- Structural basis for Ca2+-induced activation and dimerization of estrogen receptor α by calmodulin.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The homeobox gene (HOXA13) codes for a transcription factor protein that binds to AT-rich DNA sequences and controls expression of genes during embryonic morphogenesis. Here we present the NMR structure of HOXA13 homeodomain (A13DBD) bound to an 11-mer DNA duplex. A13DBD forms a dimer that binds to DNA with a dissociation constant of 7.5 nM. The A13DBD/DNA complex has a molar mass of 35 kDa consistent with two molecules of DNA bound at both ends of the A13DBD dimer. A13DBD contains an N-terminal arm (residues 324 - 329) that binds in the DNA minor groove, and a C-terminal helix (residues 362 - 382) that contacts the ATAA nucleotide sequence in the major groove. The N370 side-chain forms hydrogen bonds with the purine base of A5* (base paired with T5). Side-chain methyl groups of V373 form hydrophobic contacts with the pyrimidine methyl groups of T5, T6* and T7*, responsible for recognition of TAA in the DNA core. I366 makes similar methyl contacts with T3* and T4*. Mutants (I366A, N370A and V373G) all have decreased DNA binding and transcriptional activity. Exposed protein residues (R337, K343, and F344) make intermolecular contacts at the protein dimer interface. The mutation F344A weakens protein dimerization and lowers transcriptional activity by 76%. We conclude that the non-conserved residue, V373 is critical for structurally recognizing TAA in the major groove, and that HOXA13 dimerization is required to activate transcription of target genes.
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