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5W9Q

Zinc finger region of MBD1 in complex with CpG DNA

Summary for 5W9Q
Entry DOI10.2210/pdb5w9q/pdb
DescriptorMethyl-CpG-binding domain protein 1, dna, ZINC ION, ... (5 entities in total)
Functional Keywordszinc finger, dna-binding, cxxc3, structural genomics, structural genomics consortium, sgc, dna binding protein-dna complex, dna binding protein/dna
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus : Q9UIS9
Total number of polymer chains6
Total formula weight28921.89
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: 2017-06-23, release date: 2017-10-18, Last modification date: 2023-10-04)
Primary citationXu, 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: 29276034
DOI: 10.1016/j.str.2017.11.022
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

226707

數據於2024-10-30公開中

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