The LDL Receptor Clustering Motif Interacts with the Clathrin Terminal Domain in a Reverse Turn Conformation

@article{Kibbey1998TheLR,
  title={The LDL Receptor Clustering Motif Interacts with the Clathrin Terminal Domain in a Reverse Turn Conformation },
  author={Richard G. Kibbey and Josep Rizo and Lila M. Gierasch and Richard G. W. Anderson},
  journal={The Journal of Cell Biology},
  year={1998},
  volume={142},
  pages={59 - 67}
}
Previously the hexapeptide motif FXNPXY807 in the cytoplasmic tail of the LDL receptor was shown to be essential for clustering in clathrin-coated pits. We used nuclear magnetic resonance line-broadening and transferred nuclear Overhauser effect measurements to identify the molecule in the clathrin lattice that interacts with this hexapeptide, and determined the structure of the bound motif. The wild-type peptide bound in a single conformation with a reverse turn at residues NPVY. Tyr807Ser, a… CONTINUE READING

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