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Primary structure of human C-reactive protein

E B Oliveira, C Gotschlich, T Y Liu

    The Journal of Biological Chemistry
    |January 25, 1979
    PubMed
    Summary

    The complete amino acid sequence of human C-reactive protein (CRP) was determined, revealing 187 amino acids. Analysis showed no internal repeats, suggesting no gene duplication, and identified distant homologies to IgG and C3a anaphylotoxin.

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    Area of Science:

    • Biochemistry
    • Immunology
    • Molecular Biology

    Background:

    • Human C-reactive protein (CRP) is an acute-phase protein.
    • Understanding CRP's primary structure is crucial for elucidating its function and evolution.

    Purpose of the Study:

    • To determine the complete amino acid sequence of human CRP.
    • To analyze the primary structure for internal homology and evolutionary relationships.

    Main Methods:

    • Amino acid sequencing of human CRP.
    • Computer analysis using programs SEARCH and RELATE to compare CRP sequence with known proteins.
    • Gel filtration in guanidine HCl to determine molecular weight.

    Main Results:

    • A unique sequence of 187 amino acids was identified for human CRP.
    • The NH2-terminal residue is pyrrolidonecarboxylic acid and the COOH terminus is proline.
    • A disulfide bond involves half-cystine residues at positions 36 and 78.
    • Calculated molecular weight of 20,946 aligns with experimental data.
    • No significant internal repeating sequences were found, ruling out gene duplication.
    • Distant, statistically insignificant homologies were noted with the CH2 domain of immunoglobulin G and C3a anaphylotoxin.

    Conclusions:

    • Human CRP's primary structure does not indicate gene duplication.
    • Identified homologies are insufficient to establish a common evolutionary origin with IgG or C3a anaphylotoxin.
    • CRP and related proteins (9.5 S alpha-glycoprotein, P component, Clt) may represent a new protein superfamily.

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