They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein, and/or lipid substrates.

Sep 9, 2010 · Cys2His2 zinc finger (ZF) proteins represent the largest class of eukaryotic transcription factors. We present an approach for predicting ZF binding based on support vector machines (SVMs).

ZINC FINGER PROTEINS – STRUCTURE AND DNA RECOGNITION. The C2H2 ZF domain is the most common type of ZF and is one of the most abundantly expressed proteins in eukaryotic cells. ZFs are small, functional and independently folded domains coordinated with zinc molecules in their structure.

Jan 26, 2023 · Here we describe the screening of 49 billion protein–DNA interactions and the development of a deep-learning model, ZFDesign, that solves ZF design for any genomic target.

This review focuses on the structure, design, and applications of ZF DNA binding domains (ZFDBDs). ZFDBDs are relatively small and have been shown to penetrate the cell membrane without additional tags suggesting that they could be delivered to cells without a …

Apr 10, 2024 · To address the elucidation of 6-finger ZF (6-ZF) and DNA interactions, we modeled the 6-ZF-DNA structure using biomolecule modeling tools such as AlphaFold, Coot, and Rosetta. Rosetta has a specific application in protein-DNA modeling named the RosettaDNA application.

Nov 30, 2011 · To achieve this, we introduced amino acid substitutions into PvuII that alter Km and kcat and increase fidelity. The optimized ZF-PvuII fusion constructs cleave DNA at addressed sites with a >1000-fold preference over unaddressed PvuII sites in vitro as well as in cellula.

2 days ago · An isolated single ZF unit sometimes plays more complex roles than the DNA-binding ZF arrays. In the case of BCL11 A, mutations in ZF0 (Fig. 1A ) are pathogenic and destabilize BCL11A 38 .

Mar 22, 2018 · 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.

The readout of this sequence–dependent DNA deformation by mZFP568 involves altered alignment of the ZF array and exploits the strongly enhanced negative electrostatic potential of the DNA due to the proximity of negatively charged phosphate groups in narrower minor grooves.