title: Folding and trimerization of clathrin subunits at the triskelion hub.
abstract: The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four alpha helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.
authors.affiliation: Department of Pharmacy, University of California, San Francisco 94143.
authors.forename: I S
authors.initials: IS
authors.lastname: Näthke
authors.forename: J
authors.initials: J
authors.lastname: Heuser
authors.forename: A
authors.initials: A
authors.lastname: Lupas
authors.forename: J
authors.initials: J
authors.lastname: Stock
authors.forename: C W
authors.initials: CW
authors.lastname: Turck
authors.forename: F M
authors.initials: FM
authors.lastname: Brodsky
mesh_terms: D002966:Clathrin / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D046911:Macromolecular Substances; D008958:Models, Molecular; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D002966:Clathrin; D046911:Macromolecular Substances