Ontology highlight
ABSTRACT:
SUBMITTER: Xing Y
PROVIDER: S-EPMC2830701 | biostudies-literature | 2010 Feb
REPOSITORIES: biostudies-literature
Xing Yi Y Böcking Till T Wolf Matthias M Grigorieff Nikolaus N Kirchhausen Tomas T Harrison Stephen C SC
The EMBO journal 20091224 3
The chaperone Hsc70 drives the clathrin assembly-disassembly cycle forward by stimulating dissociation of a clathrin lattice. A J-domain containing co-chaperone, auxilin, associates with a freshly budded clathrin-coated vesicle, or with an in vitro assembled clathrin coat, and recruits Hsc70 to its specific heavy-chain-binding site. We have determined by electron cryomicroscopy (cryoEM), at about 11 A resolution, the structure of a clathrin coat (in the D6-barrel form) with specifically bound Hs ...[more]