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Molecular basis of coiled-coil formation
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Molecular basis of coiled-coil formation
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Journal Article
Molecular basis of coiled-coil formation
2007
Overview
Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed \"trigger sequence,\" that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Arginine
/ Basic-Leucine Zipper Transcription Factors
/ DNA-Binding Proteins - chemistry
/ DNA-Binding Proteins - metabolism
/ Kinetics
/ Magnetic Resonance Spectroscopy
/ Proteins
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - metabolism
