5f1s | pdb_00005f1s

Crystal structure of the teleost fish polymeric Ig receptor (pIgR) ectodomain

spinqualitylabelsall models 5f1s, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5f1s is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5d4k Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed As a first-line vertebrate immune defense, the polymeric immunoglobulin receptor (pIgR) transports polymeric IgA and IgM across epithelia to mucosal secretions, where the cleaved ectodomain (secretory component; SC) becomes a component of secretory antibodies, or when unliganded, binds and excludes bacteria. Here we report the 2.6A crystal structure of unliganded human SC (hSC) and comparisons with a 1.7A structure of teleost fish SC (tSC), an early pIgR ancestor. The hSC structure comprises five immunoglobulin-like domains (D1-D5) arranged as a triangle, with an interface between ligand-binding domains D1 and D5. Electron paramagnetic resonance measurements confirmed the D1-D5 interface in solution and revealed that it breaks upon ligand binding. Together with binding studies of mutant and chimeric SCs, which revealed domain contributions to secretory antibody formation, these results provide detailed models for SC structure, address pIgR evolution, and demonstrate that SC uses multiple conformations to protect mammals from pathogens. The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins.,Stadtmueller BM, Huey-Tubman KE, Lopez CJ, Yang Z, Hubbell WL, Bjorkman PJ Elife. 2016 Mar 4;5. pii: e10640. doi: 10.7554/eLife.10640. PMID:26943617 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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