Interaction of Two Structurally Distinct Sequence Types with the Clathrin Terminal Domain β-Propeller*

@article{Drake2001InteractionOT,
  title={Interaction of Two Structurally Distinct Sequence Types with the Clathrin Terminal Domain β-Propeller*},
  author={M. Drake and L. Traub},
  journal={The Journal of Biological Chemistry},
  year={2001},
  volume={276},
  pages={28700 - 28709}
}
  • M. Drake, L. Traub
  • Published 2001
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • The amino-terminal domain of the clathrin heavy chain, which folds into a seven-bladed β-propeller, binds directly to several endocytic proteins via short sequences based on the consensus residues LLDLD. In addition to a single LLDLD-based, type I clathrin-binding sequence, both amphiphysin and epsin contain a second, distinct sequence that is also capable of binding to clathrin directly. Here, we analyzed these sequences, which we term type II sequences, and show that the 257LMDLA sequence in… CONTINUE READING

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