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-Structure paper
Title | Structural insights into immunoglobulin M. |
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Journal, issue, pages | Science, Vol. 367, Issue 6481, Page 1014-1017, Year 2020 |
Publish date | Feb 28, 2020 |
![]() | Yaxin Li / Guopeng Wang / Ningning Li / Yuxin Wang / Qinyu Zhu / Huarui Chu / Wenjun Wu / Ying Tan / Feng Yu / Xiao-Dong Su / Ning Gao / Junyu Xiao / ![]() |
PubMed Abstract | Immunoglobulin 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), ...Immunoglobulin 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. |
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Methods | EM (single particle) |
Resolution | 3.4 Å |
Structure data | |
Chemicals | ![]() ChemComp-NAG: |
Source |
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![]() | IMMUNE SYSTEM / immunoglobulin / pentamer / transcytosis / secreted |