The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins
eLife, ISSN: 2050-084X, Vol: 5, Issue: MARCH2016, Page: e10640
2016
- 72Citations
- 146Captures
- 4Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations72
- Citation Indexes72
- 72
- CrossRef68
- Captures146
- Readers146
- 146
- Mentions4
- News Mentions3
- News3
- References1
- Wikipedia1
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Article Description
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 2.6Å crystal structure of unliganded human SC (hSC) and comparisons with a 1.7Å 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.
Bibliographic Details
10.7554/elife.10640; 10.7554/elife.10640.023; 10.7554/elife.10640.015; 10.7554/elife.10640.001; 10.7554/elife.10640.011; 10.7554/elife.10640.002; 10.7554/elife.10640.013; 10.7554/elife.10640.004; 10.7554/elife.10640.009; 10.7554/elife.10640.006; 10.7554/elife.10640.022; 10.7554/elife.10640.003
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84962255539&origin=inward; http://dx.doi.org/10.7554/elife.10640; http://www.ncbi.nlm.nih.gov/pubmed/26943617; http://dx.doi.org/10.7554/elife.10640.023; https://elifesciences.org/articles/10640#fig7; http://dx.doi.org/10.7554/elife.10640.015; https://elifesciences.org/articles/10640#abstract; http://dx.doi.org/10.7554/elife.10640.001; https://elifesciences.org/articles/10640#fig5; http://dx.doi.org/10.7554/elife.10640.011; https://elifesciences.org/articles/10640#digest; http://dx.doi.org/10.7554/elife.10640.002; https://elifesciences.org/articles/10640#fig6; http://dx.doi.org/10.7554/elife.10640.013; https://elifesciences.org/articles/10640; https://elifesciences.org/articles/10640#author-response; https://elifesciences.org/articles/10640#fig2; http://dx.doi.org/10.7554/elife.10640.004; https://elifesciences.org/articles/10640#fig4; http://dx.doi.org/10.7554/elife.10640.009; https://elifesciences.org/articles/10640#fig3; http://dx.doi.org/10.7554/elife.10640.006; https://elifesciences.org/articles/10640#decision-letter; http://dx.doi.org/10.7554/elife.10640.022; https://cdn.elifesciences.org/articles/10640/elife-10640-v2.pdf; https://cdn.elifesciences.org/articles/10640/elife-10640-v2.xml; https://elifesciences.org/articles/10640#fig1; http://dx.doi.org/10.7554/elife.10640.003; https://dx.doi.org/10.7554/elife.10640
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