title: Coiled coils meet the chaperone world.
abstract: Coiled coils are versatile structural modules that engage in a variety of cellular activities. Recent studies illuminate their role as substrate-binding elements in the chaperone cofactor prefoldin and in the AAA+ ATPases involved in protein (un)folding processes. The use of coiled coils to mediate the binding of non-native proteins represents a novel strategy in chaperone design and a new function for coiled coils.
authors.affiliation: Max-Planck-Institute for Developmental Biology, Spemannstrasse 35, D-72076 Tübingen, Germany.
authors.forename: Jörg
authors.initials: J
authors.lastname: Martin
authors.forename: Markus
authors.initials: M
authors.lastname: Gruber
authors.forename: Andrei N
authors.initials: AN
authors.lastname: Lupas
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D019843:Archaeal Proteins; D018832:Molecular Chaperones; D021122:Protein Subunits; C112806:prefoldin; D000251:Adenosine Triphosphatases