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

@inproceedings{Pinkas2017StructuralCI,
  title={Structural complexity in the KCTD family of Cullin3-dependent E3 ubiquitin ligases},
  author={Daniel M. Pinkas and Caroline E. Sanvitale and Joshua C Bufton and Fiona J. Sorrell and Nicolae Solcan and Rod Chalk and James J Doutch and Alex N Bullock},
  booktitle={The Biochemical journal},
  year={2017}
}
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… CONTINUE READING
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