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Domain binding and function: Coiled-coils (CC) function as oligomerization domains for a wide variety of proteins including structural proteins, motor proteins and transcription factors. The coiled-coil structure is conserved from viruses to plants and mammals and it has been predicted that approximately 5% of proteins encoded in sequenced genomes contain coiled-coils. Coiled-coils typically consists of two or more alpha-helices that wrap around each other with a superhelical twist. Sequences with a propensity to assume coiled-coil structures are characterized by the heptad repeat pattern (abcdefg)n, where a and d are hydrophobic, and e and g are charged or polar. Coiled-coils may interact with each other to form homotypic oligomers, or with other coiled-coil domains to form heterotypic oligomers.
Structure Reference: Nooren, I.M. et al. (1999) Nat. Struct. Biol. 6(8), 755À759.
Examples of Domain Proteins:
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| Coiled coils in the tetrameric Mnt repressor of Salmonella bacteriophage P22. | |
