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Article

AlphaFold-Predicted Structures of KCTD Proteins Unravel Previously Undetected Relationships among the Members of the Family

1
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
2
IRCCS SDN, Napoli, Via E. Gianturco 113, 80143 Naples, Italy
*
Authors to whom correspondence should be addressed.
Academic Editor: Vladimir N. Uversky
Biomolecules 2021, 11(12), 1862; https://doi.org/10.3390/biom11121862
Received: 9 November 2021 / Revised: 26 November 2021 / Accepted: 7 December 2021 / Published: 10 December 2021
(This article belongs to the Section Biomacromolecules: Proteins)
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. View Full-Text
Keywords: protein structure predictions; structure-based evolutionary trees; protein structure function protein structure predictions; structure-based evolutionary trees; protein structure function
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MDPI and ACS Style

Esposito, L.; Balasco, N.; Smaldone, G.; Berisio, R.; Ruggiero, A.; Vitagliano, L. AlphaFold-Predicted Structures of KCTD Proteins Unravel Previously Undetected Relationships among the Members of the Family. Biomolecules 2021, 11, 1862. https://doi.org/10.3390/biom11121862

AMA Style

Esposito L, Balasco N, Smaldone G, Berisio R, Ruggiero A, Vitagliano L. AlphaFold-Predicted Structures of KCTD Proteins Unravel Previously Undetected Relationships among the Members of the Family. Biomolecules. 2021; 11(12):1862. https://doi.org/10.3390/biom11121862

Chicago/Turabian Style

Esposito, Luciana, Nicole Balasco, Giovanni Smaldone, Rita Berisio, Alessia Ruggiero, and Luigi Vitagliano. 2021. "AlphaFold-Predicted Structures of KCTD Proteins Unravel Previously Undetected Relationships among the Members of the Family" Biomolecules 11, no. 12: 1862. https://doi.org/10.3390/biom11121862

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