2ocw: Difference between revisions
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New page: left|200px<br /> <applet load="2ocw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ocw" /> '''Solution structure of human secretory compo... |
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[[Image:2ocw.gif|left|200px]]<br /> | [[Image:2ocw.gif|left|200px]]<br /><applet load="2ocw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Solution structure of human secretory component'''<br /> | '''Solution structure of human secretory component'''<br /> | ||
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==Overview== | ==Overview== | ||
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. | 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 Structure== | ==About this Structure== | ||
2OCW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2OCW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OCW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: structure]] | [[Category: structure]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:47:49 2008'' | ||
