β2微球蛋白——一种游离免疫球蛋白结构域。
2 -Microglobulin--a free immunoglobulin domain.
作者信息
Peterson P A, Cunningham B A, Berggård I, Edelman G M
出版信息
Proc Natl Acad Sci U S A. 1972 Jul;69(7):1697-701. doi: 10.1073/pnas.69.7.1697.
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.
摘要
β2-微球蛋白一级结构分析表明，这种人类蛋白质在序列上与免疫球蛋白轻链恒定区（C(L)）以及免疫球蛋白G的γ1（重）链恒定区的同源区域（C(H)1、C(H)2和C(H)3）具有同源性。与C(H)3区域的同源性尤为显著。通过与免疫球蛋白轻链和重链可变区进行类似比较，未发现令人信服的同源性。β2-微球蛋白含有一个由57个氨基酸残基组成的链内二硫键环，其大小与免疫球蛋白G恒定区中发现的二硫键环相似。这些发现表明，β2-微球蛋白是一个游离的免疫球蛋白结构域，可能发挥着与免疫球蛋白G的γ1链C(H)3结构域类似的效应功能。
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