3chn | pdb_00003chn

Solution structure of human secretory IgA1

spinqualitylabelsall models 3chn Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3chn is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2qtj, 1iga, 2ocw, 3cm9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [IGHA1_HUMAN] Note=A chromosomal aberration involving IGHA1 is found in multiple myeloma (MM) cell lines. Translocation t(1;14)(q21;q32) that forms a FCRL4-IGHA1 fusion protein. Function [PIGR_HUMAN] This receptor binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment. [IGHA1_HUMAN] Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Secretory immunoglobulin A (SIgA) is the most prevalent antibody in the human body and a first line of defense in mucosal immunity. We located secretory component (SC) relative to dimeric IgA1 (dIgA1) within the SIgA1 structure using the constrained modeling of solution scattering and analytical ultracentrifugation data. The extended solution structure of dIgA1 is largely preserved within SIgA1. From conformational searches of SC locations, the best-fit SC models within SIgA1 show that SC is extended along the outermost convex edge of the Fc dimer in dIgA1. The topology of our SIgA1 structure reveals that it is able to bind to one FcalphaRI receptor molecule. SC binding to the Fc dimer confers protection to SIgA1 by the masking of proteolytically susceptible surface sites from bacterial proteases in the harsh environment of the mucosa. The models support a "zipper-like" unfolding of SC upon dIgA1 in the formation and transportation of SIgA1 into the mucosa. Location of secretory component on the Fc edge of dimeric IgA1 reveals insight into the role of secretory IgA1 in mucosal immunity.,Bonner A, Almogren A, Furtado PB, Kerr MA, Perkins SJ Mucosal Immunol. 2009 Jan;2(1):74-84. Epub 2008 Oct 8. PMID:19079336 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also IgA

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