3qmg

Structural Basis of Selective Binding of Non-Methylated CpG islands by the CXXC Domain of CFP1

spinqualitylabelsall models 3qmg, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qmg is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PEG, ZN Related: 3qmb, 3qmc, 3qmd, 3qmh, 3qmi Gene: CFP1, CGBP, CXXC1, PCCX1, PHF18 (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Function [CXXC1_HUMAN] Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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