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J Mol Evol. 1990 Jan;30(1):43-59.

Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins.

Author information

1
Department of Crystallography, Birkbeck College, University of London, United Kingdom.

Abstract

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, cytochromes c, serine proteinases, eye-lens gamma crystallins, and dinucleotide-binding domains.

PMID:
2107323
DOI:
10.1007/bf02102452
[Indexed for MEDLINE]

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