Is a leucine zipper a dimer?

Leucine zippers (bZIP) are rigid dimers of parallel extended helices. The dimer is stabilized by a coiled-coil interaction between heptad repeats of hydrophobic leucine and/or isoleucine residues along the C-terminal regions of each helix.

What is leucine zipper function?

The Leucine Zipper and the Basic DNA-Binding Domain (bZIP) This leucine zipper facilitates the dimerization of the protein by interdigitation of two leucine containing helices on different molecules and these residues form the buried subunit interface of the coiled-coil dimer.

Is leucine zipper a protein motif?

A heptad repeat of leucine residues, leucine zipper (ZIP), is an important sequence motif facilitating protein–protein interactions. ZIP forms an amphiphilic α helical structure, in which two residues that are separated by seven residues in sequence are located at nearly the same molecular surface in an α helix.

Which interaction helps the two subunits of a leucine zipper DNA binding protein are held together?

hydrophobic interactions
The two α helices containing the leucines coil together into a coiled coil in which the helices are held together predominantly by hydrophobic interactions between the leucines. The interaction between the two subunits forms a DNA binding domain made up of the basic motif region of each subunit.

Is leucine a hydrophobic?

Hydrophobic Amino Acids The nine amino acids that have hydrophobic side chains are glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), proline (Pro), phenylalanine (Phe), methionine (Met), and tryptophan (Trp).

What molecule is attached to leucine?

CHEBI:25017 – leucine A branched-chain amino acid that consists of glycine in which one of the hydrogens attached to the α-carbon is substituted by an isobutyl group.

Which amino acids are responsible for making dimer formation in leucine zippers?

The N-terminal basic region contains the amino acids lysine and arginine, which interact with the major groove of DNA in a sequence- specific manner. The C-terminus is an amphipathic α helix that dimerizes to form the leucine zipper. An amphipathic α helix has two surfaces along its length.

Which of the following best describes leucine zipper motifs?

Question Which of the following best describes leucine zipper motifs? They allow protein-protein interactions via hydrophobic bonds.