2ocw
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Solution structure of human secretory component
OverviewOverview
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.
About this StructureAbout this Structure
2OCW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of human secretory component and implications for biological function., Bonner A, Perrier C, Corthesy B, Perkins SJ, J Biol Chem. 2007 Jun 8;282(23):16969-80. Epub 2007 Apr 11. PMID:17428798
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