6LX3
Cryo-EM structure of human secretory immunoglobulin A
6LX3 の概要
エントリーDOI | 10.2210/pdb6lx3/pdb |
EMDBエントリー | 30004 |
分子名称 | Interleukin-2,Immunoglobulin heavy constant alpha 1, Immunoglobulin J chain, Polymeric immunoglobulin receptor (3 entities in total) |
機能のキーワード | immunoglobulin, dimer, transcytosis, secreted, immune system |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 208314.87 |
構造登録者 | |
主引用文献 | Wang, Y.,Wang, G.,Li, Y.,Zhu, Q.,Shen, H.,Gao, N.,Xiao, J. Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin. Cell Res., 30:602-609, 2020 Cited by PubMed Abstract: Secretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. It possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA to the mucosa. How the J-chain and pIgR/SC facilitate the assembly and secretion of SIgA remains incompletely understood. Furthermore, during the infection of Streptococcus pneumoniae, the pneumococcal adhesin SpsA hijacks pIgR/SC and SIgA to gain entry to human cells and evade host defense. How SpsA targets pIgR/SC and SIgA also remains elusive. Here we report a cryo-electron microscopy structure of the Fc region of IgA1 (Fcα) in complex with the J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present a structure of Fcα-J-SC complexed with SpsA, which uncovers the specific interactions between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on S. pneumoniae pathogenesis. PubMed: 32398862DOI: 10.1038/s41422-020-0336-3 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.15 Å) |
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