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| {{STRUCTURE_2ocw| PDB=2ocw | SCENE= }} | | {{STRUCTURE_2ocw| PDB=2ocw | SCENE= }} |
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| '''Solution structure of human secretory component'''
| | ===Solution structure of human secretory component=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17428798}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17428798 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17428798}} |
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| ==Disease== | | ==Disease== |
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| [[Category: Secretory]] | | [[Category: Secretory]] |
| [[Category: Structure]] | | [[Category: Structure]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:38:14 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:20:04 2008'' |
