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CC Domain
Structure:

Domain binding and function:
 structureCoiled-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.
Examples of Proteins: 
CC domain protein
Binding partner
EEA1 Early Endosome Protein Homotypic and heterotypic interactions
Stat1 Transcription Factor Homotypic and heterotypic interactions
Fos and Jun Heterotypic interactions

 
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