Leucine zipper: Difference between revisions
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[[Image:GCN4 Leucine Zipper.jpg|right|thumb| | [[Image:GCN4 Leucine Zipper.jpg|right|thumb|500px|The leucine zipper structure of [[GCN4]]. The leucines (yellow) and valines (magenta) form a hydrophobic zipper interaction.]] | ||
'''Leucine zippers''' are a commonly occuring [[structural motif]] in [[protein structure]]s, particularly in [[DNA]]-binding proteins, in which the amino acid [[leucine]] is repeated every seven amino acids within an [[ | '''Leucine zippers''' are a commonly occuring [[structural motif]] in [[protein structure]]s, particularly in [[DNA]]-binding proteins, in which the amino acid [[leucine]] is repeated every seven amino acids within an [[alpha-helix]] structure. Additional leucines or [[valine]]s may be present every 3rd or 4th position between the leucines. This sequence of amino acids creates an <math>\alpha</math>-helix with a very hydrophobic face, so that two such proteins can form what is termed a coiled-coil structure. Both homodimer and heterodimer leucine zippers occur naturally. | ||
Revision as of 09:53, 1 June 2008
The leucine zipper structure of GCN4. The leucines (yellow) and valines (magenta) form a hydrophobic zipper interaction.
Leucine zippers are a commonly occuring structural motif in protein structures, particularly in DNA-binding proteins, in which the amino acid leucine is repeated every seven amino acids within an alpha-helix structure. Additional leucines or valines may be present every 3rd or 4th position between the leucines. This sequence of amino acids creates an -helix with a very hydrophobic face, so that two such proteins can form what is termed a coiled-coil structure. Both homodimer and heterodimer leucine zippers occur naturally.
