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Coiled coils: a highly versatile protein folding motif.
Journal article

Coiled coils: a highly versatile protein folding motif.

  • Burkhard P M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056, Basel, Switzerland. peter.burkhard@unibas.ch
  • Stetefeld J
  • Strelkov SV
  • 2001-02-13
Published in:
  • Trends in cell biology. - 2001
Cytoskeletal Proteins
Hydrogen-Ion Concentration
Intermediate Filaments
Membrane Proteins
Protein Folding
Protein Structure, Secondary
Receptors, Immunologic
Receptors, Scavenger
SNARE Proteins
Transcription, Genetic
Vesicular Transport Proteins
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/224127
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