5V3M

mouseZFP568-ZnF1-11 in complex with DNA

5V3M の概要

• エントリーDOI: 10.2210/pdb5v3m/pdb
• 関連するPDBエントリー: 5V3G 5V3J
• 分子名称: DNA (28-MER), Zinc finger protein 568, ZINC ION, ... (5 entities in total)
• 機能のキーワード: c2h2 type zinc fingers, dna binding, transferase-dna complex, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 53918.58

構造登録者

Patel, A.,Cheng, X. (登録日: 2017-03-07, 公開日: 2018-03-07, 最終更新日: 2024-10-09)

主引用文献

Patel, A.,Yang, P.,Tinkham, M.,Pradhan, M.,Sun, M.A.,Wang, Y.,Hoang, D.,Wolf, G.,Horton, J.R.,Zhang, X.,Macfarlan, T.,Cheng, X.
DNA Conformation Induces Adaptable Binding by Tandem Zinc Finger Proteins.
Cell, 173:221-233.e12, 2018

PubMed Abstract: Tandem zinc finger (ZF) proteins are the largest and most rapidly diverging family of DNA-binding transcription regulators in mammals. ZFP568 represses a transcript of placental-specific insulin like growth factor 2 (Igf2-P0) in mice. ZFP568 binds a 24-base pair sequence-specific element upstream of Igf2-P0 via the eleven-ZF array. Both DNA and protein conformations deviate from the conventional one finger-three bases recognition, with individual ZFs contacting 2, 3, or 4 bases and recognizing thymine on the opposite strand. These interactions arise from a shortened minor groove caused by an AT-rich stretch, suggesting adaptability of ZF arrays to sequence variations. Despite conservation in mammals, mutations at Igf2 and ZFP568 reduce their binding affinity in chimpanzee and humans. Our studies provide important insights into the evolutionary and structural dynamics of ZF-DNA interactions that play a key role in mammalian development and evolution.

PubMed: 29551271
DOI: 10.1016/j.cell.2018.02.058

実験手法

X-RAY DIFFRACTION (2.091 Å)