leucine-rich repeats and immunoglobulin-like domains 1 |
leucine zipper transcription regulator 2 |
SMAD8A |
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[leucine zippers]
Leucine zippers are heptad repeats of four or five leucine residues that assume an alpha-helical configuration. These helices are held together by hydrophobic interactions between leucine residues located on one side of each helix Leucine zippers function as protein dimerization motifs. Parallel alignment of two such repeats forms a coiled-coil structure (Alber, 1993; Hurst, 1995; Landschulz et al, 1989; Vinson et al, 1989).
The leucine zipper motif occurs in many transcription factors that bind to DNA as dimeric proteins. Leucine zippers are often found within a larger protein domain known as bZIP domain [basic-leucine zipper]. This domain
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