2ocw
From Proteopedia
(New page: 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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'''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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: IgA nephropathy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173880 173880]] | ||
==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'' |
Revision as of 12:47, 23 January 2008
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Solution structure of human secretory component
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.
About this Structure
2OCW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Jan 23 14:47:49 2008
Categories: Homo sapiens | Single protein | Bonner, A. | Corthesy, B. | Perkins, S.J. | Perrier, C. | Antibody | Immunity | Immunoglobulin | Sc | Secretory | Structure
