Fifty years of coiled-coils and α-helical bundles: A close relationship between sequence and structure

• Published in: Journal of structural biology Vol. 163; no. 3; pp. 258 - 269
• Main Authors: Parry, David A.D., Fraser, R.D. Bruce, Squire, John M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2008
• Subjects: Amino Acid Sequence; Coiled coil; Crystallography, X-Ray; Hendecads; Heptads; History, 20th Century; History, 21st Century; Protein Conformation; Protein Structure, Secondary; Proteins - chemistry; Proteins - history; Sequence Homology, Amino Acid; SNARE proteins; Hendecads; Heptads; IF; SNARE proteins; Coiled coil
• ISSN: 1047-8477; 1095-8657; 1095-8657
• DOI: 10.1016/j.jsb.2008.01.016

α-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 α-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 α-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 Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years.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.