Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468), 2016 Jun; 590(11): 1663-1671.
Tipo di articolo: Letter,
Impact factor: 3.623, Impact factor a 5 anni: 3.424
Url: Non disponibile.
Parole chiave: Electron Microscopy, Protein Oligomerization, Protein Structure, Thermal Stability,
*** IBB - CNR *** IRCCS SDN, Napoli, Italy., Institute of Biostructures and Bioimaging, C.N.R., Napoli, Italy., Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici (C.I.R.C.M.S.B.), Catania, Italy., Center for Structural Systems Biology (CSSB), University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Deutsches Elektronen-Synchrotron (DESY), Hamburg, Germany., Institute of Molecular Biotechnology (IMBA), Austrian Academy of Sciences, Vienna, Austria., Research Institute of Molecular Pathology (IMP), Vienna, Austria.,
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.
402 Records (390 escludendo Abstract e Conferenze). Impact factor totale: 1601.608 (1555.147 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 1640.334 (1585.284 escludendo Abstract e Conferenze).