The study identifies the structural and sequence homology between C-reactive protein and C1t, proposing the term 'pentraxin' for this family of proteins with cyclic pentameric symmetry.
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Nomenclature shift to pentraxins may unify CRP research; leaves open functional validation in cardiovascular models.
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.
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Osmand et al. (1977) studied this question.
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