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Free keywords:
VIRAL MEMBRANE-FUSION; ALPHA-HELICAL BARRELS; GCN4 LEUCINE-ZIPPER; AMINO-ACID-SEQUENCE; CRYSTAL-STRUCTURE; INFLUENZA HEMAGGLUTININ; MUREIN-LIPOPROTEIN; ESCHERICHIA-COLI; PROTEIN; PARALLEL
Abstract:
alpha-Helical coiled coils were described more than 60 years ago as simple, repetitive structures mediating oligomerization and mechanical stability. Over the past 20 years, however, they have emerged as one of the most diverse protein folds in nature, enabling many biological functions beyond mechanical rigidity, such as membrane fusion, signal transduction, and solute transport. Despite this great diversity, their structures can be described by parametric equations, making them uniquely suited for rational protein design. Far from having been exhausted as a source of structural insight and a basis for functional engineering, coiled coils are poised to become even more important for protein science in the coming decades.
