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6VTX

Crystal structure of human KLF4 zinc finger DNA binding domain in complex with NANOG DNA

6VTX の概要
エントリーDOI10.2210/pdb6vtx/pdb
分子名称Krueppel-like factor 4, DNA (5'-D(*AP*GP*GP*GP*GP*GP*TP*GP*TP*GP*CP*C)-3'), DNA (5'-D(*GP*GP*CP*AP*CP*AP*CP*CP*CP*CP*CP*T)-3'), ... (6 entities in total)
機能のキーワードklf4, zinc finger, dna binding domain, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数3
化学式量合計17545.31
構造登録者
Sharma, R.,Sharma, S.,Choi, K.J.,Ferreon, A.C.M.,Ferreon, J.C.,Sankaran, B.,MacKenzie, K.R.,Kim, C. (登録日: 2020-02-13, 公開日: 2021-09-01, 最終更新日: 2023-10-11)
主引用文献Sharma, R.,Choi, K.J.,Quan, M.D.,Sharma, S.,Sankaran, B.,Park, H.,LaGrone, A.,Kim, J.J.,MacKenzie, K.R.,Ferreon, A.C.M.,Kim, C.,Ferreon, J.C.
Liquid condensation of reprogramming factor KLF4 with DNA provides a mechanism for chromatin organization.
Nat Commun, 12:5579-5579, 2021
Cited by
PubMed Abstract: Expression of a few master transcription factors can reprogram the epigenetic landscape and three-dimensional chromatin topology of differentiated cells and achieve pluripotency. During reprogramming, thousands of long-range chromatin contacts are altered, and changes in promoter association with enhancers dramatically influence transcription. Molecular participants at these sites have been identified, but how this re-organization might be orchestrated is not known. Biomolecular condensation is implicated in subcellular organization, including the recruitment of RNA polymerase in transcriptional activation. Here, we show that reprogramming factor KLF4 undergoes biomolecular condensation even in the absence of its intrinsically disordered region. Liquid-liquid condensation of the isolated KLF4 DNA binding domain with a DNA fragment from the NANOG proximal promoter is enhanced by CpG methylation of a KLF4 cognate binding site. We propose KLF4-mediated condensation as one mechanism for selectively organizing and re-organizing the genome based on the local sequence and epigenetic state.
PubMed: 34552088
DOI: 10.1038/s41467-021-25761-7
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.14 Å)
構造検証レポート
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件を2026-04-15に公開中

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