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 | |||||||||
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![]() solution structure of the second cut ___domain of human satb2 | |||||||||
Identifiers | |||||||||
Symbol | CUT | ||||||||
Pfam | PF02376 | ||||||||
InterPro | IPR003350 | ||||||||
SCOP2 | 1wh6 / SCOPe / SUPFAM | ||||||||
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References
edit- ^ 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.
- ^ 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.