Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure.
alpha-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of functions that they exhibit. The coiled coils are based on a heptad (7-residue), hendecad (11-residue) or a related quasi-repeat of apolar residues in the sequences of the alpha-helical regions involved. Most of these, however, display one or more sequence discontinuities known as stutters or stammers. The resulting coiled coils vary in length, in the number of chains participating, in the relative polarity of the contributing alpha-helical regions (parallel or antiparallel), and in the pitch length and handedness of the supercoil (left- or right-handed). Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years. An important development has been the recognition that the delightful simplicity that exists between sequence and structure, and between structure and function, allows coiled coils with specialized features to be designed de novo.
Parry
David A D
DA
Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand. d.parry@massey.ac.nz
Fraser
R D Bruce
RD
Squire
John M
JM
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D049673:History, 20th Century; D049674:History, 21st Century; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000266:history; D017386:Sequence Homology, Amino Acid
D011506:Proteins