Structural complexity in the KCTD family of Cullin3-dependent E3 ubiquitin ligases

@article{Pinkas2017StructuralCI,
  title={Structural complexity in the KCTD family of Cullin3-dependent E3 ubiquitin ligases},
  author={D. Pinkas and C. Sanvitale and Joshua C Bufton and F. Sorrell and N. Solcan and R. Chalk and J. Doutch and A. Bullock},
  journal={Biochemical Journal},
  year={2017},
  volume={474},
  pages={3747 - 3761}
}
Members of the potassium channel tetramerization domain (KCTD) family are soluble non-channel proteins that commonly function as Cullin3 (Cul3)-dependent E3 ligases. Solution studies of the N-terminal BTB domain have suggested that some KCTD family members may tetramerize similarly to the homologous tetramerization domain (T1) of the voltage-gated potassium (Kv) channels. However, available structures of KCTD1, KCTD5 and KCTD9 have demonstrated instead pentameric assemblies. To explore other… Expand
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References

SHOWING 1-10 OF 68 REFERENCES
Molecular organization of the cullin E3 ligase adaptor KCTD11.
Pentameric assembly of potassium channel tetramerization domain-containing protein 5.
Structural Basis for Cul3 Protein Assembly with the BTB-Kelch Family of E3 Ubiquitin Ligases*
Protein partners of KCTD proteins provide insights about their functional roles in cell differentiation and vertebrate development.
...
1
2
3
4
5
...