Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles.

@article{Gruschus2004StructureOT,
  title={Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles.},
  author={James M. Gruschus and Chae Jung Han and Tsvika Greener and James A. Ferretti and Lois E. Greene and Evan Eisenberg},
  journal={Biochemistry},
  year={2004},
  volume={43 11},
  pages={
          3111-9
        }
}
The three-dimensional structure of the C-terminal 20 kDa portion of auxilin, which consists of the clathrin binding region and the C-terminal J-domain, has been determined by NMR. Auxilin is an Hsp40 family protein that catalytically supports the uncoating of clathrin-coated vesicles through recruitment of Hsc70 in an ATP hydrolysis-driven process. This 20 kDa auxilin construct contains the minimal sequential region required to uncoat clathrin-coated vesicles catalytically. The tertiary… CONTINUE READING
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