Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins.
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.
Johnson
M S
MS
Department of Crystallography, Birkbeck College, University of London, United Kingdom.
Sutcliffe
M J
MJ
Blundell
T L
TL
D000595:Amino Acid Sequence; D000818:Animals; D003459:Crystallins / Q000235:genetics / Q000648:ultrastructure; D005914:Globins / Q000235:genetics / Q000648:ultrastructure; D006801:Humans; D007136:Immunoglobulins / Q000235:genetics / Q000648:ultrastructure; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009711:Nucleotides / Q000378:metabolism; D010802:Phylogeny; D011487:Protein Conformation; D011506:Proteins / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000235:genetics
D003459:Crystallins; D007136:Immunoglobulins; D009711:Nucleotides; D011506:Proteins; D005914:Globins; D012697:Serine Endopeptidases