Related Experiment Video
Updated: May 8, 2026

Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
Published on: March 25, 2015
Structure based design of protein linkers for zinc finger nuclease
Priya Anand1, Alexander Schug, Wolfgang Wenzel
1Institute of Nanotechnology, Karlsruhe Institute of Technology, 76021 Karlsruhe, Germany.
Abstract:
Zinc finger nucleases are a promising tool to edit DNA in many biological applications, in particular for gene knockout. Despite many efforts the number of genes that can be effectively targeted with ZFNs remains severely limited, as available constructs cannot address arbitrary gene sequences. Here, we develop a novel concept to significantly enhance the number of DNA sequences that can be targeted by ZFN. Using an efficient computational model, we provide an extensive library of possible linker molecules between individual zinc finger motifs in the construct that can skip up to 10 base pairs between adjacent zinc finger recognition sites in the DNA sequence, which increases the number of genes that can be efficiently targeted by more than an order of magnitude.
Related Concept Videos
Ligand Binding and Linkage
Ligand Binding and Linkage
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Cytoskeletal Linker Proteins - Plakins
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.

