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...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1977-02, Vol.74 (2), p.739-743
Main Authors: Osmand, Alexander P., Friedenson, Bernard, Gewurz, Henry, Painter, Robert H., Hofmann, Theo, Shelton, Emma
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Amyloids
Animals
C-Reactive Protein - isolation & purification
Complement C1
Complement System Proteins
Cyanogen Bromide
Humans
Immunoglobulins
Immunology
Macromolecular Substances
Microscopy, Electron
Molecular weight
Molecules
Peptide Fragments - analysis
Protein Conformation
Protein subunits
Proteins
Rabbits
Species Specificity
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.74.2.739