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. 1972 Jul;69(7):1697–1701. doi: 10.1073/pnas.69.7.1697

β2-Microglobulin—A Free Immunoglobulin Domain

Per A Peterson 1, Bruce A Cunningham 1, Ingemar Berggård , Gerald M Edelman 1
PMCID: PMC426781  PMID: 4558655

Abstract

Analysis of the primary structure of β2-microglobulin indicates that this human protein is homologous in sequence to the constant portion of immunoglobulin light chains (CL), and to the homology regions (CH1, CH2, and CH3) of the constant portion of γ1 (heavy) chains of immunoglobulin G. Homology with the CH3 region is particularly striking. No convincing homology could be demonstrated by similar comparisons with the variable regions of immunoglobulin light and heavy chains. β2-Microglobulin contains an intrachain disulfide loop of 57 amino-acid residues that is similar in size to disulfide loops found in the constant regions of immunoglobulin G. These findings suggest that β2-microglobulin is a free immunoglobulin domain, possibly serving an effector function similar to that of the CH3 domain of γ1 chains of immunoglobulin G.

Keywords: light and heavy chain, amino-acid sequence

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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