5f1s

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'''Unreleased structure'''
 
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The entry 5f1s is ON HOLD until Paper Publication
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==Crystal structure of the teleost fish polymeric Ig receptor (pIgR) ectodomain==
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<StructureSection load='5f1s' size='340' side='right' caption='[[5f1s]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5f1s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F1S FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d4k|5d4k]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f1s OCA], [http://pdbe.org/5f1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f1s RCSB], [http://www.ebi.ac.uk/pdbsum/5f1s PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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As a first-line vertebrate immune defense, the polymeric immunoglobulin receptor (pIgR) transports polymeric IgA and IgM across epithelia to mucosal secretions, where the cleaved ectodomain (secretory component; SC) becomes a component of secretory antibodies, or when unliganded, binds and excludes bacteria. Here we report the 2.6A crystal structure of unliganded human SC (hSC) and comparisons with a 1.7A structure of teleost fish SC (tSC), an early pIgR ancestor. The hSC structure comprises five immunoglobulin-like domains (D1-D5) arranged as a triangle, with an interface between ligand-binding domains D1 and D5. Electron paramagnetic resonance measurements confirmed the D1-D5 interface in solution and revealed that it breaks upon ligand binding. Together with binding studies of mutant and chimeric SCs, which revealed domain contributions to secretory antibody formation, these results provide detailed models for SC structure, address pIgR evolution, and demonstrate that SC uses multiple conformations to protect mammals from pathogens.
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Authors: Stadtmueller, B.M., Bjorkman, P.J.
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The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins.,Stadtmueller BM, Huey-Tubman KE, Lopez CJ, Yang Z, Hubbell WL, Bjorkman PJ Elife. 2016 Mar 4;5. pii: e10640. doi: 10.7554/eLife.10640. PMID:26943617<ref>PMID:26943617</ref>
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Description: Crystal structure of the teleost fish polymeric Ig receptor (pIgR) ectodomain
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Bjorkman, P.J]]
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<div class="pdbe-citations 5f1s" style="background-color:#fffaf0;"></div>
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[[Category: Stadtmueller, B.M]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bjorkman, P J]]
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[[Category: Stadtmueller, B M]]
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[[Category: Immune system]]
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[[Category: Mucosal immunity]]
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[[Category: Polymeric ig-binding protein]]
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[[Category: Secretory component]]

Revision as of 03:49, 11 May 2016

Crystal structure of the teleost fish polymeric Ig receptor (pIgR) ectodomain

5f1s, resolution 1.75Å

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