Zinc finger domains assist the binding of the protein to nucleic acids.

It has a zinc finger domain and is highly conserved throughout many eukaryotic organisms.

The finger domain functions to bind the nucleotide triphosphate with the template base.

This gene encodes a protein containing zinc finger domains.

The signature of the C2H2-type zinc finger domain is:

Many of its orthologs, paralogs, and neighboring genes have been shown to possess zinc finger domains.

It includes two pairs of conserved histidines and one asparagine that create a zinc finger domain.

The zinc finger domain is believed to bind to the RNA molecule.

ZZ-type zinc finger domains are found in:

One of these zinc finger domains bind the carboxy-terminal domain of Vps28 and the other associates with ubiquitin.

The parallel selection (Fig. 1 (A)) approach assumes that the individual zinc finger domains are functionally independent.

The zinc finger domains do not appear to bind nucleosomes well and can be displaced by FOX factors.

The encoded protein contains a distinguishing putative zinc finger domain with a repeating cys-his motif.

Two zinc finger domains are looped into the GLUE domain of Vps36.

SUZ12 is component of the PCR2 and it consists of a zinc finger domain.

The following is a schematic representation of the structure of the RING finger domain:

Examples of human genes which encode proteins containing a RING finger domain include:

The protein encoded by this gene contains a RING finger domain and acts as a transcription factor.

Another conserved domain within the Mdm2 protein is a Zinc finger domain, the function of which is poorly understood.

Yoon showed that mutating the Gli zinc finger domain inhibited the proteins effect proving its role as a transcription factor.

RoXaN is a protein that contains tetratricopeptide repeat and leucine-aspartate repeat as well as zinc finger domains.

Standard ZFNs fuse the cleavage domain to the C-terminus of each zinc finger domain.

In molecular biology the MYND-type zinc finger domain is a conserved protein domain.

The amino acid structure of the EGR-1 zinc finger domain is given in this table, using the single letter amino acid code.

In molecular biology, the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold.