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• W3195621306 abstract "Modern proteins have been shown to share evolutionary relationships via subdomain-sized fragments. The assembly of such fragments through duplication and recombination events led to the complex structures and functions we observe today. We previously implemented a pipeline that identified more than 1,000 of these fragments that are shared by different protein folds and developed a web interface to analyze and search for them. This resource named Fuzzle helps structural and evolutionary biologists to identify and analyze conserved parts of a protein but it also provides protein engineers with building blocks for example to design proteins by fragment combination. Here, we describe a new version of this web resource that was extended to include ligand information. This addition is a significant asset to the database since now protein fragments that bind specific ligands can be identified and analyzed. Often the mode of ligand binding is conserved in proteins thereby supporting a common evolutionary origin. The same can now be explored for subdomain-sized fragments within this database. This ligand binding information can also be used in protein engineering to graft binding pockets into other protein scaffolds or to transfer functional sites via recombination of a specific fragment. Fuzzle 2.0 is freely available at https://fuzzle.uni-bayreuth.de/2.0 ." @default.
• W3195621306 created "2021-08-30" @default.
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• W3195621306 date "2021-08-18" @default.
• W3195621306 modified "2023-09-24" @default.
• W3195621306 title "Fuzzle 2.0: Ligand Binding in Natural Protein Building Blocks" @default.
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• W3195621306 doi "https://doi.org/10.3389/fmolb.2021.715972" @default.
• W3195621306 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8416435" @default.
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