Synopsis
Understanding protein structure and function requires understanding of the modular nature of proteins and their native folds. Most proteins are made up of one to several sequence segments or domains that share a common core fold and often function and in multidomain proteins are connected by typically unstructured linker sequences. Invention, duplication, sharing, and remodeling of domains have been constant processes throughout proteome evolution. Domains are classified by fold, conserved sequence, and conserved function into fold families and fold superfamilies. Surprisingly, the sum of domain fold space is highly limited and appears to be fully represented by as few as 1,200 folds, about 2,000 fold superfamilies, and roughly 4,000 fold families. Examination of fold family invention, loss, and sharing has revealed much about the history and associations of the three superkingdoms of life. Fold family diversification begins early in evolutionary history with rapid invention...
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Vandergon, T.L. (2014). Protein Domain Structure Evolution. In: Bell, E. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6436-5_19-2
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DOI: https://doi.org/10.1007/978-1-4614-6436-5_19-2
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