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- W3214974852 endingPage "12776" @default.
- W3214974852 startingPage "12776" @default.
- W3214974852 abstract "Immunoglobulin G (IgG) is currently the most studied immunoglobin class and is frequently used in antibody therapeutics in which its beneficial effector functions are exploited. IgG is composed of two heavy chains and two light chains, forming the basic antibody monomeric unit. In contrast, immunoglobulin A (IgA) and immunoglobulin M (IgM) are usually assembled into dimers or pentamers with the contribution of joining (J)-chains, which bind to the secretory component (SC) of the polymeric Ig receptor (pIgR) and are transported to the mucosal surface. IgA and IgM play a pivotal role in various immune responses, especially in mucosal immunity. Due to their structural complexity, 3D structural study of these molecules at atomic scale has been slow. With the emergence of cryo-EM and X-ray crystallographic techniques and the growing interest in the structure-function relationships of IgA and IgM, atomic-scale structural information on IgA-Fc and IgM-Fc has been accumulating. Here, we examine the 3D structures of IgA and IgM, including the J-chain and SC. Disulfide bridging and N-glycosylation on these molecules are also summarized. With the increasing information of structure-function relationships, IgA- and IgM-based monoclonal antibodies will be an effective option in the therapeutic field." @default.
- W3214974852 created "2021-12-06" @default.
- W3214974852 creator A5011203970 @default.
- W3214974852 creator A5016698604 @default.
- W3214974852 creator A5052716791 @default.
- W3214974852 date "2021-11-26" @default.
- W3214974852 modified "2023-10-04" @default.
- W3214974852 title "3D Structures of IgA, IgM, and Components" @default.
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