Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller.

@article{Drake2001InteractionOT,
  title={Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller.},
  author={Matthew T. Drake and Linton M. Traub},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 31},
  pages={28700-9}
}
The amino-terminal domain of the clathrin heavy chain, which folds into a seven-bladed beta-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 (257)LMDLA… CONTINUE READING

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