Summary
A distance measure that reflects the dissimilarity among structures has been developed on the basis of the three-dimensional structures of similar proteins, this being totally independent of sequence in the sense that only the relative spatial positions of mainchain alpha-carbon atoms need be known. This procedure leads to phyletic relationships that are in general correlated with the sequence phylogenies based on residue type. Such relationships among known protein three-dimensional structures are also a useful aid to their classification and selection in knowledge-based modeling using homologous structures. We have applied this approach to six homologous sets of proteins: immunoglobulin fragments, globins, cytochromesc, serine proteinases, eye-lens gamma crystallins, and dinucleotide-binding domains.
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Johnson, M.S., Sutcliffe, M.J. & Blundell, T.L. Molecular anatomy: Phyletic relationships derived from three-dimensional structures of proteins. J Mol Evol 30, 43–59 (1990). https://doi.org/10.1007/BF02102452
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DOI: https://doi.org/10.1007/BF02102452