Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins).
- 1 February 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (2) , 739-743
- https://doi.org/10.1073/pnas.74.2.739
Abstract
Partial amino acid sequences of rabbit C-reactive protein [CRP], a peptide derived from human CrP by CNBr cleavage, and human C1t[t subcomponent of the 1st complement component] were determined. Extensive sequence homology between these proteins establish their evolutionary relationships. Examination of C-reactive proteins by negative-stain EM revealed that the protein is composed of 5 subunits arranged in cyclic symmetry. This structure is similar to 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.This publication has 22 references indexed in Scilit:
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