6kxs
From Proteopedia
Cryo-EM structure of human IgM-Fc in complex with the J chain and the ectodomain of pIgR
Structural highlights
FunctionIGJ_HUMAN Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component.[UniProtKB:P01592] Publication Abstract from PubMedImmunoglobulin M (IgM) plays a pivotal role in both humoral and mucosal immunity. Its assembly and transport depend on the joining chain (J-chain) and the polymeric immunoglobulin receptor (pIgR), but the underlying molecular mechanisms of these processes are unclear. We report a cryo-electron microscopy structure of the Fc region of human IgM in complex with the J-chain and pIgR ectodomain. The IgM-Fc pentamer is formed asymmetrically, resembling a hexagon with a missing triangle. The tailpieces of IgM-Fc pack into an amyloid-like structure to stabilize the pentamer. The J-chain caps the tailpiece assembly and bridges the interaction between IgM-Fc and the polymeric immunoglobulin receptor, which undergoes a large conformational change to engage the IgM-J complex. These results provide a structural basis for the function of IgM. Structural insights into immunoglobulin M.,Li Y, Wang G, Li N, Wang Y, Zhu Q, Chu H, Wu W, Tan Y, Yu F, Su XD, Gao N, Xiao J Science. 2020 Feb 28;367(6481):1014-1017. doi: 10.1126/science.aaz5425. Epub 2020, Feb 6. PMID:32029689[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Li Y | Wang G | Xiao J
