Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins).
Partial amino acid sequences of rabbit C-reactive protein, a peptide derived from human C-reactive protein by cyanogen bromide cleavage, and the C1t subcomponent of the human complement component C1 have been determined. Extensive sequence homology between these proteins establish their evolutionary relationships. In addition, examination of C-reactive proteins by negative-stain electron microscopy revealed that the protein is composed of five subunits arranged in cyclic symmetry. This structure is similar to that reported for both C1t and the amyloid P-component. The extensive structural relationship suggests similar or overlapping functions and the term pentraxin is proposed to describe these homologous proteins.
D000595:Amino Acid Sequence; D000818:Animals; D002097:C-Reactive Protein / Q000302:isolation & purification; D003172:Complement C1; D003165:Complement System Proteins; D003488:Cyanogen Bromide; D006801:Humans; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D011817:Rabbits; D013045:Species Specificity
D003172:Complement C1; D046911:Macromolecular Substances; D010446:Peptide Fragments; D003165:Complement System Proteins; D002097:C-Reactive Protein; D003488:Cyanogen Bromide
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