3QMG
Structural Basis of Selective Binding of Non-Methylated CpG islands by the CXXC Domain of CFP1
Summary for 3QMG
Entry DOI | 10.2210/pdb3qmg/pdb |
Related | 3QMB 3QMC 3QMD 3QMH 3QMI |
Descriptor | CpG-binding protein, 5'-D(*GP*CP*CP*AP*AP*CP*GP*GP*TP*GP*GP*C)-3', 5'-D(*GP*CP*CP*AP*CP*CP*GP*TP*TP*GP*GP*C)-3', ... (6 entities in total) |
Functional Keywords | structural genomics consortium, sgc, protein-dna complex, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus speckle: Q9P0U4 |
Total number of polymer chains | 3 |
Total formula weight | 17092.67 |
Authors | Xu, C.,Bian, C.,MacKenzie, F.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2011-02-04, release date: 2011-02-23, Last modification date: 2023-09-13) |
Primary citation | 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, 2:227-227, 2011 Cited by PubMed Abstract: 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. PubMed: 21407193DOI: 10.1038/ncomms1237 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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