5VC9
Zinc finger of human CXXC4 in complex with CpG DNA
Summary for 5VC9
| Entry DOI | 10.2210/pdb5vc9/pdb |
| Descriptor | CpG DNA, CXXC-type zinc finger protein 4, UNKNOWN ATOM OR ION, ... (5 entities in total) |
| Functional Keywords | cxxc, dna, structural genomics, structural genomics consortium, sgc, dna binding protein |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cytoplasm : Q9H2H0 |
| Total number of polymer chains | 6 |
| Total formula weight | 26139.11 |
| Authors | Liu, K.,Xu, C.,Tempel, W.,Walker, J.R.,Arrowsmith, C.H.,Bountra, C.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2017-03-31, release date: 2017-06-28, Last modification date: 2024-04-03) |
| Primary citation | Xu, C.,Liu, K.,Lei, M.,Yang, A.,Li, Y.,Hughes, T.R.,Min, J. DNA Sequence Recognition of Human CXXC Domains and Their Structural Determinants. Structure, 26:85-95.e3, 2018 Cited by PubMed Abstract: The CXXC domain, first identified as the reader of unmodified CpG dinucleotide, plays important roles in epigenetic regulation by targeting various activities to CpG islands. Here we systematically measured and compared the DNA-binding selectivities of all known human CXXC domains by different binding assays, and complemented the existing function-based classification of human CXXC domains with a classification based on their DNA selectivities. Through a series of crystal structures of CXXC domains with DNA ligands, we unravel the molecular mechanisms of how these CXXC domains, including single CXXC domains and tandem CXXC-PHD domains, recognize distinct DNA ligands, which further supports our classification of human CXXC domains and also provides insights into selective recruitment of chromatin modifiers to their respective targets via CXXC domains recognizing different genomic DNA sequences. Our study facilitates the understanding of the relationship between the DNA-binding specificities of the CXXC proteins and their biological functions. PubMed: 29276034DOI: 10.1016/j.str.2017.11.022 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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