Secretory component (SC) in association with polymeric IgA (pIgA) forms secretory IgA, the major antibody active at mucosal surfaces. SC also exists in the free form, with innate-like neutralizing properties against pathogens. Free SC consists of five glycosylated variable (V)-type Ig domains (D1–D5), whose structure was determined by x-ray and neutron scattering, ultracentrifugation, and modeling. With a radius of gyration of 3.53–3.63 nm, a length of 12.5 nm, and a sedimentation coefficient of 4.0 S, SC possesses an unexpected compact structure. Constrained scattering modeling based on up to 13,000 trial models shows that SC adopts a J-shaped structure in which D4 and D5 are folded back against D2 and D3. The seven glycosylation sites are located on one side of SC, leaving known IgA-binding motifs free to interact with pIgA. This work represents the first analysis of the three-dimensional structure of full-length free SC and paves the way to a better understanding of the association between SC and its potential ligands, i.e. pIgA and pathogenic-associated motifs.
Solution Structure of Human Secretory Component and Implications for Biological Function*
Alexandra Bonner,C. Perrier,B. Corthésy,S. Perkins
Published 2007 in Journal of Biological Chemistry
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- Publication year
2007
- Venue
Journal of Biological Chemistry
- Publication date
2007-06-08
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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