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The Structure and Topology of α-Helical Coiled Coils

  • Andrei N. LupasEmail author
  • Jens Bassler
  • Stanislaw Dunin-Horkawicz
Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 82)

Abstract

α-Helical coiled coils constitute one of the most diverse folds yet described. They range in length over two orders of magnitude; they form rods, segmented ropes, barrels, funnels, sheets, spirals, and rings, which encompass anywhere from two to more than 20 helices in parallel or antiparallel orientation; they assume different helix crossing angles, degrees of supercoiling, and packing geometries. This structural diversity supports a wide range of biological functions, allowing them to form mechanically rigid structures, provide levers for molecular motors, project domains across large distances, mediate oligomerization, transduce conformational changes and facilitate the transport of other molecules. Unlike almost any other protein fold known to us, their structure can be computed from parametric equations, making them an ideal model system for rational protein design. Here we outline the principles by which coiled coils are structured, review the determinants of their folding and stability, and present an overview of their diverse architectures.

Keywords

Leucine Zipper Coiled Coil Heptad Repeat Hydrophilic Residue Antiparallel Orientation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer International Publishing AG 2017

Authors and Affiliations

  • Andrei N. Lupas
    • 1
    Email author
  • Jens Bassler
    • 1
  • Stanislaw Dunin-Horkawicz
    • 2
  1. 1.Department of Protein EvolutionMax Planck Institute for Developmental BiologyTübingenGermany
  2. 2.Structural Bioinformatics Laboratory, Centre of New TechnologiesUniversity of WarsawWarsawPoland

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