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

D A Parry, R D Fraser, JM Squire

Research output: Contribution to journalArticle (Academic Journal)peer-review

192 Citations (Scopus)

Abstract

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 Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years.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.
Translated title of the contributionFifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure
Original languageEnglish
Pages (from-to)258 - 269
Number of pages12
JournalJournal of Structural Biology
Volume163
DOIs
Publication statusPublished - Sep 2008

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