Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation.

@article{Strelkov2002AnalysisOA,
  title={Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation.},
  author={Sergei V. Strelkov and Peter Burkhard},
  journal={Journal of structural biology},
  year={2002},
  volume={137 1-2},
  pages={
          54-64
        }
}
Alpha-helical coiled coils represent a widespread protein structure motif distinguished by a seven-residue periodicity of apolar residues in the primary sequence. A characteristic "knobs-into-holes" packing of these residues into a hydrophobic core results in a superhelical, usually left-handed, rope of two or more alpha-helices. Such a geometry can be parameterized. For this purpose, a new computer program, TWISTER, was developed. With the three-dimensional coordinates as input, TWISTER uses… 
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241 Citations

Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure.

A seven-helix coiled coil

It is demonstrated that heptad repeats containing four hydrophobic positions can direct assembly of complex, higher-order coiled-coil structures with rich diversity for close packing of α-helices.

Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction.

A library of coiled-coil domains: from regular bundles to peculiar twists

SamCC-Turbo, a software for fully automated, per-residue measurement of coiled coils, is developed and a comprehensive atlas of ∼50 000 coiled-coil regions is generated, which features precise measurements as well as decomposes coil structures into fragments characterized by various degrees of supercoiling.

Designability landscape reveals sequence features that define axial helix rotation in four-helical homo-oligomeric antiparallel coiled-coil structures.

Antiparallel Four-Stranded Coiled Coil Specified by a 3-3-1 Hydrophobic Heptad Repeat

α/β coiled coils

The results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold.

The Structure and Topology of α-Helical Coiled Coils

The principles by which coiled coils are structured are outlined, the determinants of their folding and stability are reviewed, and an overview of their diverse architectures are presented.

How sequence directs bending in tropomyosin and other two‐stranded alpha‐helical coiled coils

  • Jerry H. Brown
  • Chemistry
    Protein science : a publication of the Protein Society
  • 2010
Comparison of tropomyosin structures determined in independent crystal environments provides further evidence for the concept that sequence directs the bending of the coiled coil, but that crystal environment is at least as important as sequence for determining the magnitude of bending.

Simultaneous formation of right- and left-handed anti-parallel coiled-coil interfaces by a coil2 fragment of human lamin A.

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20 References

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