Journal article
Structural Complexity in the KCTD Family of Cullin3-Dependent E3 Ubiquitin Ligases
- Abstract:
-
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 ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Bibliographic Details
- Publisher:
- Portland Press Publisher's website
- Journal:
- Biochemical Journal Journal website
- Volume:
- 474
- Issue:
- 22
- Pages:
- 3747-3761
- Publication date:
- 2017-09-28
- Acceptance date:
- 2017-09-25
- DOI:
- EISSN:
-
1470-8728
- ISSN:
-
0264-6021
- Pmid:
-
28963344
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:732843
- UUID:
-
uuid:f092490a-7780-4519-b56e-ea3a84efed69
- Local pid:
- pubs:732843
- Deposit date:
- 2017-10-09
Terms of use
- Copyright holder:
- ©2017 Pinkas, et al
- Copyright date:
- 2017
- Notes:
- This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY).
- Licence:
- CC Attribution (CC BY)
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