Leucine zipper

Leucine zipper
A protein structural motif common in transcription factors. Leucine zipper is formed by two proteins (homodimmer or heterodimmer) and binds to DNA.
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Leucine zipper: A motif found in certain proteins in which Leu residues are evenly spaced through an a-helical region, such that they would end up on the same face of the helix. Dimers can form between two such proteins.
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leucine zipper A protein structural motif involved in protein-protein interactions in many eukaryotic regulatory proteins (C/EBP prototype). Contain a repeat structure: Leu residues in every seventh position, causes a large amount of DNA to loop out.
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Over the past few years, it has become apparent that members of the CNC (cap 'n' collar)-basic leucine zipper family of transcription factors are principal mediators of defensive responses to redox stress.
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Leucine zippers function in associating the transcription factors with each other.
Basic-helix-loop-helix (bHLH) bind DNA with two alpha helices containing basic amino acid residues which are linked by a loop and are typically dimeric.
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α helices have particular significance in DNA binding motifs, including helix-turn-helix motifs, leucine zipper motifs and zinc finger motifs.
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: Common sites on different proteins which facilitate their binding to DNA. Examples are leucine zipper and zinc finger proteins. Any such protein is called DNA-binding protein.
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