David Auble
Alpha helical coiled coils are ubiquitous. There is extensive experimental and theoretical data bearing on how they form and how their specificity and stability are determined. The parallel interaction of right-handed α-helices wrapped in a left-handed supecoil was originally proposed by Crick in the early 1950s to explain diffraction data obtained in studies of fibrous proteins like keratin. Here you can see how alpha helical coiled coils in transcription factors, now referred to as leucine zippers, mediate dimerization. The interactions that direct association of the helices are primarily hydrophobic, although electrostatic interactions can also dictate specificity. These images are derived from 2zta (Gcn4 leucine zipper core), 1ysa (Gcn4 bzip-DNA complex), and 1d66 (Gal4 DBD-DNA complex).
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