Journal
FEBS LETTERS
Volume 590, Issue 11, Pages 1663-1671Publisher
WILEY-BLACKWELL
DOI: 10.1002/1873-3468.12203
Keywords
electron microscopy; protein oligomerization; protein structure; thermal stability
Funding
- Regione Campania (Bando POR per la Realizzazione della Rete delle Biotecnologie in Campania - progetto FARMABIONET)
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Potassium channel tetramerization domain-containing (KCTD) proteins are involved in fundamental physio-pathological processes. Here, we report an analysis of the oligomeric state of the Bric-a-brack, Tram-track, Broad complex (BTB) domains of seven distinct KCTDs belonging to five major clades of the family evolution tree. Despite their functional and sequence variability, present electron microscopy data highlight the occurrence of well-defined pentameric states for all domains. Our data also show that these states coexist with alternative forms which include open pentamers. Thermal denaturation analyses conducted using KCTD1 as a model suggest that, in these proteins, different domains cooperate to their overall stability. Finally, negative-stain electron micrographs of KCTD6 BTB in complex with Cullin3 show the presence of assemblies with a five-pointed pinwheel shape.
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