In molecular biology, the CUT ___domain (also known as ONECUT) is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, which is often found downstream of the CUT ___domain. Proteins display two modes of DNA binding, which hinge on the homeodomain and on the linker that separates it from the CUT ___domain, and two modes of transcriptional stimulation, which hinge on the homeodomain.[1][2]

CUT
solution structure of the second cut ___domain of human satb2
Identifiers
SymbolCUT
PfamPF02376
InterProIPR003350
SCOP21wh6 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References

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  1. ^ Lannoy VJ, Burglin TR, Rousseau GG, Lemaigre FP (May 1998). "Isoforms of hepatocyte nuclear factor-6 differ in DNA-binding properties, contain a bifunctional homeodomain, and define the new ONECUT class of homeodomain proteins". J. Biol. Chem. 273 (22): 13552–62. doi:10.1074/jbc.273.22.13552. PMID 9593691.
  2. ^ Yamasaki, K.; Akiba, T.; Yamasaki, T.; Harata, K. (2007). "Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB1". Nucleic Acids Research. 35 (15): 5073–5084. doi:10.1093/nar/gkm504. PMC 1976457. PMID 17652321.
This article incorporates text from the public ___domain Pfam and InterPro: IPR003350