6ue8

Structure of tetrameric sIgA complex (Class 1)

Loading... Status: waiting for Mol* initialization Structural highlights 6ue8 is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: BMA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IGHA2_HUMAN Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system. Publication Abstract from PubMed Secretory immunoglobulin A (sIgA) represents the immune system's first-line of defense against mucosal pathogens. IgAs are transported across the epithelium, as dimers and higher-order polymers, by the polymeric immunoglobulin receptor (pIgR). Upon reaching the luminal side, sIgAs mediate host protection and pathogen neutralization. In recent years, an increasing amount of attention has been given to IgA as a novel therapeutic antibody. Despite extensive studies sIgA structures have remained elusive. Here, we determine the atomic-resolution structures of dimeric, tetrameric, and pentameric IgA-Fc linked by the joining chain (JC) and in complex with the secretory component of the pIgR. We suggest a mechanism where the JC templates IgA oligomerization and imparts asymmetry for pIgR binding and transcytosis. This framework will inform the design of future IgA-based therapeutics. Structure of the secretory immunoglobulin A core.,Kumar N, Arthur CP, Ciferri C, Matsumoto ML Science. 2020 Feb 6. pii: science.aaz5807. doi: 10.1126/science.aaz5807. PMID:32029686 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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