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-Structure paper
タイトル | CD5L associates with IgM via the J chain. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 8397, Year 2024 |
掲載日 | 2024年9月27日 |
著者 | Yuxin Wang / Chen Su / Chenggong Ji / Junyu Xiao / |
PubMed 要旨 | CD5 antigen-like (CD5L), also known as Spα or AIM (Apoptosis inhibitor of macrophage), emerges as an integral component of serum immunoglobulin M (IgM). However, the molecular mechanism underlying ...CD5 antigen-like (CD5L), also known as Spα or AIM (Apoptosis inhibitor of macrophage), emerges as an integral component of serum immunoglobulin M (IgM). However, the molecular mechanism underlying the interaction between IgM and CD5L has remained elusive. In this study, we present a cryo-electron microscopy structure of the human IgM pentamer core in complex with CD5L. Our findings reveal that CD5L binds to the joining chain (J chain) in a Ca-dependent manner and further links to IgM via a disulfide bond. We further corroborate recently published data that CD5L reduces IgM binding to the mucosal transport receptor pIgR, but does not impact the binding of the IgM-specific receptor FcμR. Additionally, CD5L does not interfere with IgM-mediated complement activation. These results offer a more comprehensive understanding of IgM and shed light on the function of the J chain in the immune system. |
リンク | Nat Commun / PubMed:39333069 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.39 - 3.41 Å |
構造データ | EMDB-37936, PDB-8wyr: EMDB-37937, PDB-8wys: |
化合物 | ChemComp-NAG: ChemComp-CA: |
由来 |
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キーワード | IMMUNE SYSTEM / immunoglobulin / CD5 antigen-like / pentamer |