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Clathrin coats at 21 Å resolution: a cellular assembly designed to recycle multiple membrane receptors

TitleClathrin coats at 21 Å resolution: a cellular assembly designed to recycle multiple membrane receptors
Publication TypeJournal Article
Year of Publication1998
AuthorsSmith, CJ, Grigorieff N, Pearse BM
Refereed DesignationRefereed
JournalEMBO J
Date PublishedSep 1
ISBN Number0261-4189 (Print)
Accession Number9724631
KeywordsAdaptor Protein Complex alpha Subunits, Adaptor Proteins, Vesicular Transport, Animals, Clathrin/metabolism/*ultrastructure, Coated Vesicles/*ultrastructure, Cryoelectron Microscopy, Image Processing, Computer-Assisted, Membrane Proteins/metabolism/*ultrastructure, Models, Structural, Protein Binding, Swine

We present a map at 21 A resolution of clathrin assembled into cages with the endocytic adaptor complex, AP-2. The map was obtained by cryo-electron microscopy and single-particle reconstruction. It reveals details of the packing of entire clathrin molecules as they interact to form a cage with two nested polyhedral layers. The proximal domains of each triskelion leg depart from a cage vertex in a skewed orientation, forming a slightly twisted bundle with three other leg domains. Thus, each triskelion contributes to two connecting edges of the polyhedral cage. The clathrin heavy chains continue inwards under the vertices with local 3-fold symmetry, the terminal domains contributing to 'hook-like' features which form an intermediate network making possible contacts with the surface presented by the inner adaptor shell. A node of density projecting inwards from the vertex may correspond to the C-termini of clathrin heavy chains which form a protrusion on free triskelions at the vertex. The inter-subunit interactions visible in this map provide a structural basis for considering the assembly of clathrin coats on a membrane and show the contacts which will need to be disrupted during disassembly.

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