3cm9: Difference between revisions

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<StructureSection load='3cm9' size='340' side='right'caption='[[3cm9]]' scene=''>
<StructureSection load='3cm9' size='340' side='right'caption='[[3cm9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cm9]] is a 10 chain structure with 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=3CM9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CM9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cm9]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CM9 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r70|1r70]], [[3chn|3chn]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray solution scattering</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3cm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cm9 OCA], [http://pdbe.org/3cm9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cm9 RCSB], [http://www.ebi.ac.uk/pdbsum/3cm9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cm9 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cm9 OCA], [https://pdbe.org/3cm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cm9 RCSB], [https://www.ebi.ac.uk/pdbsum/3cm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cm9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PIGR_HUMAN 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.  
[https://www.uniprot.org/uniprot/PIGR_HUMAN 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cm9 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cm9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Secretory IgA (SIgA) is the most prevalent human antibody and is central to mucosal immunity. It exists as two subclasses, SIgA1 and SIgA2, where SIgA2 has a shorter hinge joining the Fab and Fc regions. Both forms of SIgA are predominantly dimeric and contain an additional protein called the secretory component (SC) that is attached during the secretory process and is believed to protect SIgA in harsh mucosal conditions. Here we locate the five SC domains relative to dimeric IgA2 within SIgA2 using constrained scattering modeling. The x-ray and sedimentation parameters showed that SIgA2 has an extended solution structure. The constrained modeling of SIgA2 was initiated using two IgA2 monomers that were positioned according to our best fit solution structure for dimeric IgA1. SC was best located along the convex edge of the Fc-Fc region. The best fit models showed that SIgA2 is significantly nonplanar in its structure, in distinction to our previous near planar SIgA1 structure. Both the shorter IgA2 hinges and the presence of SC appear to displace the four Fab regions out of the Fc plane in SIgA2. This may explain the noncovalent binding of SC in some SIgA2 molecules. This nonplanar structure is predicted to result in specific immune properties for SIgA2 and SIgA1. It may explain differences observed between the SIgA1 and SIgA2 subclasses in terms of their interactions with antigens, susceptibility to proteases, effects on receptors, and distribution in different tissues. The different structures account for the prevalence of both forms in mucosal secretions.
The nonplanar secretory IgA2 and near planar secretory IgA1 solution structures rationalize their different mucosal immune responses.,Bonner A, Almogren A, Furtado PB, Kerr MA, Perkins SJ J Biol Chem. 2009 Feb 20;284(8):5077-87. Epub 2008 Dec 23. PMID:19109255<ref>PMID:19109255</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3cm9" style="background-color:#fffaf0;"></div>
==See Also==
*[[IgA|IgA]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Almogren, A]]
[[Category: Almogren A]]
[[Category: Bonner, A]]
[[Category: Bonner A]]
[[Category: Furtado, P B]]
[[Category: Furtado PB]]
[[Category: Kerr, M A]]
[[Category: Kerr MA]]
[[Category: Perkins, S J]]
[[Category: Perkins SJ]]
[[Category: Constrained modelling]]
[[Category: Glycoprotein]]
[[Category: Iga]]
[[Category: Immune system]]
[[Category: Immunoglobulin c region]]
[[Category: Immunoglobulin domain]]
[[Category: Membrane]]
[[Category: Mucosal immunity]]
[[Category: Phosphoprotein]]
[[Category: Secreted]]
[[Category: Secretory iga1]]
[[Category: Secretory iga2]]
[[Category: Transmembrane]]
[[Category: X-ray and neutron scattering]]

Latest revision as of 12:36, 21 February 2024

Solution Structure of Human SIgA2Solution Structure of Human SIgA2

Structural highlights

3cm9 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.
Method:X-ray solution scattering
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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