About Coiled-Coil Domain:
A coiled-coil is a type of structural motif that is found within proteins whereby alpha-helices coil together like rope strands. Read on to discover more about them.
A coiled-coil is found in proteins in all of life’s three kingdoms. Coiled-coil domains of some proteins are relatively invariant in length and sequence, betraying a functional and structural role for amino acids along the full length of the coiled-coil.
Coiled-Coil Domain Structure
The most common types are trimers and dimers.
There are some coiled-coils that are conserved in length but when it comes to sequence, they are divergent, meaning they function as molecular spacers. When in this capacity, the architecture of organelles is influenced by coiled‐coil proteins. Examples include the Golgi and centrioles, and also permitting the tethering of carrier vesicles.
Coiled-Coil Domain Structure Function
A lot of coiled-coil type proteins play a vital role in key biological functions, for example, gene expression regulation. Notable examples are the oncoproteins c-jun and c-FOS, as well as tropomyosin, which is the muscle protein.
Specialized coiled-coils, for example, those that are located in motor proteins have the capability of propagating conformational adaptions along their length, which regulate motor processivity and cargo binding.
Coiled-coil domains have been recognized in enzymes too, where they operate as molecular rulers, with catalytic activities being positioned at fixed distances.
While there has been a lot of discussion into coiled-coils for their ability to scaffold and nucleate big macromolecular complexes, there is not enough structural evidence to substantiate this claim, and so more research needs to be done.