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Home > A. Molecular pathology > coiled-coil proteins

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coiled-coil proteins

The alpha-helical coiled coil is one of the principal subunit oligomerization motifs in proteins. Its most characteristic feature is a heptad repeat pattern of primarily apolar residues that constitute the oligomer interface.

Despite its simplicity, it is a highly versatile folding motif: coiled-coil-containing proteins exhibit a broad range of different functions related to the specific ’design’ of their coiled-coil domains.

The architecture of a particular coiled-coil domain determines its oligomerization state, rigidity and ability to function as a molecular recognition system. Much progress has been made towards understanding the factors that determine

Features

- coiled-coil formation
- coiled-coil stability
- protein folding
- protein oligomerization

References

- Burkhard P, Stetefeld J, Strelkov SV. Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 2001 Feb;11(2):82-8. PMID: 11166216