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Title
Coiled-coils: The long and short of it
AuthorLeonard, Thomas A. ; Trübestein, Linda
Published in
BioEssays, Hoboken, 2016, Vol. 38, Issue 9, page 903-916
PublishedHoboken : Wiley-Blackwell, 2016
LanguageEnglish
Document typeJournal Article
Keywords (EN)allostery / coiled-coil / molecular ruler / molecular spacer / scaffold / kinetochore-microtubule attachment / eubacterium thermotoga-maritima / dynein motor domain / crystal-structure / protein-kinase / structural basis / membrane curvature / dynactin complex / molecular ruler / copi vesicles
Project-/ReportnumberP 28135-B26
URNurn:nbn:at:at-ubmuw:3-1377 Persistent Identifier (URN)
DOI10.1002/bies.201600062 
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 The work is publicly available
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Abstract (English)

Coiled-coils are found in proteins throughout all three kingdoms of life. Coiled-coil domains of some proteins are almost invariant in sequence and length, betraying a structural and functional role for amino acids along the entire length of the coiled-coil. Other coiled-coils are divergent in sequence, but conserved in length, thereby functioning as molecular spacers. In this capacity, coiled-coil proteins influence the architecture of organelles such as centrioles and the Golgi, as well as permit the tethering of transport vesicles. Specialized coiled-coils, such as those found in motor proteins, are capable of propagating conformational changes along their length that regulate cargo binding and motor processivity. Coiled-coil domains have also been identified in enzymes, where they function as molecular rulers, positioning catalytic activities at fixed distances. Finally, while coiled-coils have been extensively discussed for their potential to nucleate and scaffold large macromolecular complexes, structural evidence to substantiate this claim is relatively scarce.

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CC-BY-License (4.0)Creative Commons Attribution 4.0 International License