AlphaFold-Predicted Structures of KCTD Proteins Unravel Previously Undetected Relationships among the Members of the Family(291 views) Esposito L, Balasco N, Smaldone G, Berisio R, Ruggiero A, Vitagliano L
Biomolecules (ISSN: 2218-273xlinking), 2021 Dec 10; 11(12): N/D-N/D.
Paper type: Journal Article, Research Support, Non-U. S. Gov',
Impact factor: 6.06, 5-year impact factor: 6.06
Url: Not available.
Keywords: Humans, Models, Molecular, Phylogeny, Protein Binding, Protein Domains, Protein Folding, Protein Structure, Secondary, Chemistry, Metabolism, Protein Structure Function, Protein Structure Predictions, Structure-Based Evolutionary Trees,
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy., IRCCS SDN, Napoli, Via E. Gianturco 113, 80143 Naples, Italy.,
References: Not available.
AlphaFold-Predicted Structures of KCTD Proteins Unravel Previously Undetected Relationships among the Members of the Family
One of the most striking features of KCTD proteins is their involvement in apparently unrelated yet fundamental physio-pathological processes. Unfortunately, comprehensive structure-function relationships for this protein family have been hampered by the scarcity of the structural data available. This scenario is rapidly changing due to the release of the protein three-dimensional models predicted by AlphaFold (AF). Here, we exploited the structural information contained in the AF database to gain insights into the relationships among the members of the KCTD family with the aim of facilitating the definition of the structural and molecular basis of key roles that these proteins play in many biological processes. The most important finding that emerged from this investigation is the discovery that, in addition to the BTB domain, the vast majority of these proteins also share a structurally similar domain in the C-terminal region despite the absence of general sequence similarities detectable in this region. Using this domain as reference, we generated a novel and comprehensive structure-based pseudo-phylogenetic tree that unraveled previously undetected similarities among the protein family. In particular, we generated a new clustering of the KCTD proteins that will represent a solid ground for interpreting their many functions.
AlphaFold-Predicted Structures of KCTD Proteins Unravel Previously Undetected Relationships among the Members of the Family
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