Homology modelling of the catalytic domain of early mammalian protein C: evolution of structural features.
By means of a novel cDNA-based strategy employing the maximum parsimony principle, we have previously deduced probable amino acid sequences for the catalytic domains of the early mammalian ancestors of each of the five extant vitamin K-dependent serine proteases of coagulation, and for their common ancestor from a still earlier stage of vertebrate evolution. In the present study, we employed one of these sequences to construct a molecular model of the catalytic domain of early mammalian protein C and to explore its functional architecture. Following the domain's progression from the common ancestor of the vitamin K-dependent serine proteases toward extant human protein C, this novel application of homology modelling to a reconstructed amino acid sequence has allowed us to trace the evolution of structural features in a vital coagulation protein.
Wacey
A I
AI
Thrombosis Research Institute, London, UK.
Krawczak
M
M
Kemball-Cook
G
G
Cooper
D N
DN
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019143:Evolution, Molecular; D006801:Humans; D008322:Mammals; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011486:Protein C / Q000737:chemistry* / Q000235:genetics*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity
D011486:Protein C