3qmh
Structural Basis of Selective Binding of Non-Methylated CpG islands (DNA-TCGA) by the CXXC Domain of CFP1Structural Basis of Selective Binding of Non-Methylated CpG islands (DNA-TCGA) by the CXXC Domain of CFP1
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 PubMedCFP1 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
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