coiledcoilmediated

Coiled-coil mediated refers to cellular interactions driven by coiled-coil motifs in proteins. A coiled-coil is formed when two or more alpha-helices wrap around each other to create a stable supercoil. The defining feature is a heptad repeat in the amino-acid sequence, typically denoted a–g, with hydrophobic residues commonly at positions a and d that form the core, and charged residues at e and g that can form salt bridges to stabilize the assembly. The helices can align in parallel or antiparallel orientations and can be homo- or hetero-oligomeric.

These motifs function as modular dimerization or oligomerization domains and are found in diverse proteins, where they mediate protein-protein interactions, structural assembly, and signaling. In biological systems they contribute to vesicle fusion (as in SNARE proteins), cytoskeletal organization (e.g., tropomyosin), and transcriptional regulation (leucine-zipper-containing transcription factors).

Because coiled-coil formation is primarily determined by sequence patterns, many coiled-coil regions can be predicted from protein sequences using specialized algorithms, and their interactions can be studied with biophysical methods and structural biology. Engineered coiled-coil domains have been developed as synthetic dimerization modules to control protein assembly in research and biotechnology, with applications in nanomaterials, gene regulation, and synthetic biology.