2 -Microglobulin--a free immunoglobulin domain.
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Journal: 1972/September - Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
PUBMED: 4558655
Abstract:
Analysis of the primary structure of beta(2)-microglobulin indicates that this human protein is homologous in sequence to the constant portion of immunoglobulin light chains (C(L)), and to the homology regions (C(H)1, C(H)2, and C(H)3) of the constant portion of gamma1 (heavy) chains of immunoglobulin G. Homology with the C(H)3 region is particularly striking. No convincing homology could be demonstrated by similar comparisons with the variable regions of immunoglobulin light and heavy chains. beta(2)-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 beta(2)-microglobulin is a free immunoglobulin domain, possibly serving an effector function similar to that of the C(H)3 domain of gamma1 chains of immunoglobulin G.
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Proc Natl Acad Sci U S A 69(7): 1697-1701
PMID: 4558655

β<sub>2</sub>-Microglobulin—A Free Immunoglobulin Domain

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.

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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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The University of Lund, Lund, Sweden
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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.
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