6nce
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Crystal structure of the human FOXN3 DNA binding domain in complex with a forkhead DNA sequence
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Structural highlights
FunctionFOXN3_HUMAN Acts as a transcriptional repressor. May be involved in DNA damage-inducible cell cycle arrests (checkpoints).[1] Publication Abstract from PubMedTranscription factors (TFs) control gene expression by binding DNA recognition sites in genomic regulatory regions. Although most forkhead TFs recognize a canonical forkhead (FKH) motif, RYAAAYA, some forkheads recognize a completely different (FHL) motif, GACGC. Bispecific forkhead proteins recognize both motifs, but the molecular basis for bispecific DNA recognition is not understood. We present co-crystal structures of the FoxN3 DNA binding domain bound to the FKH and FHL sites, respectively. FoxN3 adopts a similar conformation to recognize both motifs, making contacts with different DNA bases using the same amino acids. However, the DNA structure is different in the two complexes. These structures reveal how a single TF binds two unrelated DNA sequences and the importance of DNA shape in the mechanism of bispecific recognition. Bispecific Forkhead Transcription Factor FoxN3 Recognizes Two Distinct Motifs with Different DNA Shapes.,Rogers JM, Waters CT, Seegar TCM, Jarrett SM, Hallworth AN, Blacklow SC, Bulyk ML Mol Cell. 2019 Feb 22. pii: S1097-2765(19)30039-5. doi:, 10.1016/j.molcel.2019.01.019. PMID:30826165[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 06:49, 11 October 2023.