CC Domain

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 α-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

1. Nooren, I.M. et al. (1999) Nat. Struct. Biol. 6(8), 755–759.

Examples of Domain Proteins

Binding Examples

CC Domain Proteins	Binding Partners
EEA1 Early Endosome Protein	Homotypic and heterotypic interactions
Stat1 Transcription Factor	Homotypic and heterotypic interactions
Fos and Jun	Heterotypic interactions