Coiled coils: a highly versatile protein folding motif

Trends Cell Biol. 2001 Feb;11(2):82-8. doi: 10.1016/s0962-8924(00)01898-5.


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 coiled-coil formation and stability. Here we discuss this highly versatile protein folding and oligomerization motif with regard to its structural architecture and how this is related to its biological functions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cytoskeletal Proteins / chemistry*
  • Cytoskeletal Proteins / metabolism
  • Hydrogen-Ion Concentration
  • Intermediate Filaments / chemistry*
  • Intermediate Filaments / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Protein Folding*
  • Protein Structure, Secondary* / physiology
  • Receptors, Immunologic / chemistry
  • Receptors, Immunologic / metabolism
  • Receptors, Scavenger
  • SNARE Proteins
  • Transcription, Genetic / physiology
  • Vesicular Transport Proteins*


  • Cytoskeletal Proteins
  • Membrane Proteins
  • Receptors, Immunologic
  • Receptors, Scavenger
  • SNARE Proteins
  • Vesicular Transport Proteins