Structural basis of ubiquitylation.

@article{Vandemark2002StructuralBO,
  title={Structural basis of ubiquitylation.},
  author={Andrew P Vandemark and Christopher P Hill},
  journal={Current opinion in structural biology},
  year={2002},
  volume={12 6},
  pages={822-30}
}
The attachment of the small protein ubiquitin to other proteins, a process known as ubiquitylation, is a widespread form of post-translational modification that regulates numerous cellular functions in eukaryotes. Ubiquitylation is performed by complexes of E2 and E3 enzymes that are assembled and select substrates via a series of protein-protein interactions. Recent structure determinations of the ubiquitylation machinery have revealed some of the various protein-protein interfaces involved. 
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Structure of the Tsg 101 UEV domain in complex with its peptide binding site in the HIV - 1 p 6 protein

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