{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Blaber M"],"pubmed_abstract":["β-trefoil proteins exhibit an approximate C<sub>3</sub> rotational symmetry. An analysis of the secondary structure for members of this diverse superfamily of proteins indicates that it is comprised of remarkably conserved β-strands and highly-divergent turn regions. A fundamental \"minimal\" architecture can be identified that is devoid of heterogenous and extended turn regions, and is conserved among all family members. Conversely, the different functional families of β-trefoils can potentially be identified by their unique turn patterns (or turn \"signature\"). Such analyses provide clues as to the evolution of the β-trefoil family, suggesting a folding/stability role for the β-strands and a functional role for turn regions. This viewpoint can also guide <i>de novo</i> protein design of β-t"],"journal":["Frontiers in molecular biosciences"],"pagination":["889943"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9062101"],"repository":["biostudies-literature"],"pubmed_title":["Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function."],"pmcid":["PMC9062101"],"pubmed_authors":["Blaber M"],"additional_accession":[]},"is_claimable":false,"name":"Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function.","description":"β-trefoil proteins exhibit an approximate C<sub>3</sub> rotational symmetry. An analysis of the secondary structure for members of this diverse superfamily of proteins indicates that it is comprised of remarkably conserved β-strands and highly-divergent turn regions. A fundamental \"minimal\" architecture can be identified that is devoid of heterogenous and extended turn regions, and is conserved among all family members. Conversely, the different functional families of β-trefoils can potentially be identified by their unique turn patterns (or turn \"signature\"). Such analyses provide clues as to the evolution of the β-trefoil family, suggesting a folding/stability role for the β-strands and a functional role for turn regions. This viewpoint can also guide <i>de novo</i> protein design of β-t","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-05-18T12:05:30.361Z","creation":"2025-04-05T20:39:28.538Z"},"accession":"S-EPMC9062101","cross_references":{"pubmed":["35517858"],"doi":["10.3389/fmolb.2022.889943"]}}