Structure and ubiquitin binding of the ubiquitin-interacting motif.

@article{Fisher2003StructureAU,
  title={Structure and ubiquitin binding of the ubiquitin-interacting motif.},
  author={Robert D. Fisher and Bin Wang and Steven L. Alam and Daniel S. Higginson and Howard Robinson and Wesley I. Sundquist and Christopher P Hill},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 31},
  pages={
          28976-84
        }
}
Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules. Here, we report the crystal structure and ubiquitin binding properties of one such module, the ubiquitin-interacting motif (UIM). We found that UIM peptides from several proteins involved… CONTINUE READING

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