Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure: a prediction of the structure of the catalytic domain of protein kinases.
The secondary structure and elements of tertiary structure have been predicted for the catalytic domain of protein kinases using a method that extracts structural information from the patterns of conservation and variation in an alignment of homologous proteins. The central features of this structural prediction are: (a) the catalytic domains of protein kinases do not incorporate a Rossmann fold; (b) the core of the structure is founded on beta sheets built from pairs of bent antiparallel beta strands; (c) five helices, including an especially long helix (alignment positions 129-152) that lie on the outside of the folded core. These proteins are important in many aspects of metabolic regulation.
Benner
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SA
Laboratory for Organic Chemistry, E.T.H., Zurich, Switzerland.
Gerloff
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D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D014644:Genetic Variation; D006801:Humans; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D011494:Protein Kinases