Structural highlights
Function
[CXXC1_HUMAN] Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG.[1]
Publication Abstract from PubMed
CFP1 is a CXXC domain-containing protein and an essential component of the SETD1 histone H3K4 methyltransferase complex. CXXC domain proteins direct different chromatin-modifying activities to various chromatin regions. Here, we report crystal structures of the CFP1 CXXC domain in complex with six different CpG DNA sequences. The crescent-shaped CFP1 CXXC domain is wedged into the major groove of the CpG DNA, distorting the B-form DNA, and interacts extensively with the major groove of the DNA. The structures elucidate the molecular mechanism of the non-methylated CpG-binding specificity of the CFP1 CXXC domain. The CpG motif is confined by a tripeptide located in a rigid loop, which only allows the accommodation of the non-methylated CpG dinucleotide. Furthermore, we demonstrate that CFP1 has a preference for a guanosine nucleotide following the CpG motif.
The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain.,Xu C, Bian C, Lam R, Dong A, Min J Nat Commun. 2011 Mar;2:227. PMID:21407193[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu C, Bian C, Lam R, Dong A, Min J. The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain. Nat Commun. 2011 Mar;2:227. PMID:21407193 doi:10.1038/ncomms1237
- ↑ Xu C, Bian C, Lam R, Dong A, Min J. The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain. Nat Commun. 2011 Mar;2:227. PMID:21407193 doi:10.1038/ncomms1237
