title: Coiled-coils: The long and short of it.
abstract: 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.
authors: Department of Structural and Computational Biology, Max F. Perutz Laboratories (MFPL), Vienna Biocenter (VBC), Vienna, Austria.
authors: Linda
authors: L
authors: Truebestein
authors: Department of Structural and Computational Biology, Max F. Perutz Laboratories (MFPL), Vienna Biocenter (VBC), Vienna, Austria.|Department of Medical Biochemistry, Medical University of Vienna, Vienna, Austria.
authors: Thomas A
authors: TA
authors: Leonard
mesh_terms: D000818:Animals; D001419:Bacteria / Q000378:metabolism; D056890:Eukaryota / Q000378:metabolism; D006801:Humans; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*
chemical_list: D011506:Proteins
keywords: allostery; coiled-coil; molecular ruler; molecular spacer; scaffold