Coiled-Coil

The English term coiled-coil, loosely translated as winding screw or double helix refers to a protein structural motif. A double spiral is a helix, which is in turn wound into a helix having a larger radius.

A coiled-coil is a stable, linear domain consisting of at least two Einzelhelices. In general, these are α - helices. This Einzelhelices are wound around each other in a multi-helix. Thus, it is in each of these twisted Einzelhelices a double helix. The term itself is a not so with that a coiled-coil consists of several Einzelhelices.

Characteristic of coiled coils is the so-called Heptadenmuster, standing by the hydrophobic amino acid residues at the 1st and 4th position of a seven -amino acid portion. The hydrophobic interaction of these amino acids, the coiled-coil structure is stabilized.

A coiled-coil of the most common structures are the bZIP domain (including leucine zipper ).

Coiled - coil motifs are found in many proteins, such as transcription factors or in participating in vesicle proteins. They probably still often a function as a spacer. For some proteins, they also contribute to dimer formation.

Gp41 hexamer, which enables the entry of HIV into the cell

The transcription factor CREB

Proteins with coiled-coil

• Lamin and other intermediate filaments
• Certain myosins
• Collagen