leucine zipper

In place of a coiled coil, a leucine zipper was found.

Both changes, although conserved in five different species, are deviations from the classical leucine zipper model.

Neural retina-specific leucine zipper proteins also belong to this family.

In addition to these domains there are two leucine zippers starting at base pairs 484 and 505 suggesting protein-protein interaction.

A Leucine zipper pattern was found beginning at Lys113 and ending at Lys134.

Here he examined the c-Fos leucine zipper dimerisation domain to elucidate its function.

There are three areas within the expressed protein that possibly have motifs; leucine zipper within a coiled-coil.

They realized that the myc protein bore several telltale shapes, including one evocatively called a leucine zipper.

Localization of this protein to the centrosome requires three leucine zippers in the central coiled-coil domain.

In addition it has two leucine zippers and an RCC1 domain that represents other potential protein-protein interactions.

The first class is comprised of short coiled-coil domains of six or seven heptad repeats, also called leucine zippers.

A leucine zipper, aka leucine scissors, is a common three-dimensional structural motif in proteins.

The other subclass does not contain a TIR and instead has a leucine zipper region at its amino terminal.

Max binds to itself and to other transcription factors through its leucine zipper to form homo- and hetero-dimers respectively.

Leucine zippers are found in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes.

Each half of a leucine zipper consists of a short alpha-helix with a leucine residue at every seventh position.

This member contains a nuclear targeting signal sequence, a protein kinase domain, a leucine zipper motif, and a highly conservative 13-consecutive-histidine repeat.

The leucine zipper of this protein mediates dimerization with members of the Jun family of proteins.

SREBPs belong to the basic-helix-loop-helix leucine zipper class of transcription factors.

In addition to this characteristic forkhead-box domain, the protein contains a polyglutamine tract, a zinc finger and a leucine zipper.

C/EBPα dimerizes via the leucine zipper.

We found that transcriptional activation domain 3 and the leucine zipper were not required for prolongation of either G1 or S (Fig 7).

- ATF6 (activating transcription factor 6) is a basic leucine zipper transcription factor.

The interacting domains in PMS2 have heptad repeats that are characterstic of leucine zipper proteins.

The product of this gene has three leucine zipper motifs bracketed by two basic domains that are all required for DNA binding.