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5K5J

Homo sapiens CCCTC-binding factor (CTCF) ZnF5-8 and DNA complex structure in space group P41212

Summary for 5K5J
Entry DOI10.2210/pdb5k5j/pdb
Related5K5H 5K5I 5K5L
DescriptorTranscriptional repressor CTCF, DNA (5'-D(*CP*CP*CP*TP*GP*CP*TP*GP*GP*CP*AP*AP*C)-3'), DNA (5'-D(*TP*TP*GP*CP*CP*AP*GP*CP*AP*GP*GP*GP*G)-3'), ... (7 entities in total)
Functional Keywordsccctc-binding factor, ctcf, zinc finger, transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight22084.76
Authors
Hashimoto, H.,Cheng, X. (deposition date: 2016-05-23, release date: 2017-05-24, Last modification date: 2023-09-27)
Primary citationHashimoto, H.,Wang, D.,Horton, J.R.,Zhang, X.,Corces, V.G.,Cheng, X.
Structural Basis for the Versatile and Methylation-Dependent Binding of CTCF to DNA.
Mol. Cell, 66:711-720.e3, 2017
Cited by
PubMed Abstract: The multidomain CCCTC-binding factor (CTCF), containing a tandem array of 11 zinc fingers (ZFs), modulates the three-dimensional organization of chromatin. We crystallized the human CTCF DNA-binding domain in complex with a known CTCF-binding site. While ZF2 does not make sequence-specific contacts, each finger of ZF3-7 contacts three bases of the 15-bp consensus sequence. Each conserved nucleotide makes base-specific hydrogen bonds with a particular residue. Most of the variable base pairs within the core sequence also engage in interactions with the protein. These interactions compensate for deviations from the consensus sequence, allowing CTCF to adapt to sequence variations. CTCF is sensitive to cytosine methylation at position 2, but insensitive at position 12 of the 15-bp core sequence. These differences can be rationalized structurally. Although included in crystallizations, ZF10 and ZF11 are not visible, while ZF8 and ZF9 span the backbone of the DNA duplex, conferring no sequence specificity but adding to overall binding stability.
PubMed: 28529057
DOI: 10.1016/j.molcel.2017.05.004
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.287 Å)
Structure validation

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數據於2024-11-06公開中

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