6gbh: Difference between revisions

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'''Unreleased structure'''


The entry 6gbh is ON HOLD  until Paper Publication
==Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1==
<StructureSection load='6gbh' size='340' side='right' caption='[[6gbh]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gbh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GBH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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=6gbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbh OCA], [http://pdbe.org/6gbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gbh RCSB], [http://www.ebi.ac.uk/pdbsum/6gbh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbh ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human gastric pathogen Helicobacter pylori is a major causative agent of gastritis, peptic ulcer disease, and gastric cancer. As part of its adhesive lifestyle, the bacterium targets members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family by the conserved outer membrane adhesin HopQ. The HopQ-CEACAM1 interaction is associated with inflammatory responses and enables the intracellular delivery and phosphorylation of the CagA oncoprotein via a yet unknown mechanism. Here, we generated crystal structures of HopQ isotypes I and II bound to the N-terminal domain of human CEACAM1 (C1ND) and elucidated the structural basis of H. pylori specificity toward human CEACAM receptors. Both HopQ alleles target the beta-strands G, F, and C of C1ND, which form the trans dimerization interface in homo- and heterophilic CEACAM interactions. Using SAXS, we show that the HopQ ectodomain is sufficient to induce C1ND monomerization and thus providing H. pylori a route to influence CEACAM-mediated cell adherence and signaling events.


Authors: Moonens, K., Kruse, T., Gerhard, M., Remaut, H.
Helicobacter pylori adhesin HopQ disrupts trans dimerization in human CEACAMs.,Moonens K, Hamway Y, Neddermann M, Reschke M, Tegtmeyer N, Kruse T, Kammerer R, Mejias-Luque R, Singer BB, Backert S, Gerhard M, Remaut H EMBO J. 2018 Jun 1. pii: embj.201798665. doi: 10.15252/embj.201798665. PMID:29858229<ref>PMID:29858229</ref>


Description: Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6gbh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gerhard, M]]
[[Category: Kruse, T]]
[[Category: Moonens, K]]
[[Category: Remaut, H]]
[[Category: Remaut, H]]
[[Category: Moonens, K]]
[[Category: Adhesin]]
[[Category: Kruse, T]]
[[Category: Cell adhesion]]
[[Category: Gerhard, M]]
[[Category: Helicobacter outer membrane protein]]
[[Category: Helicobacter pylori]]
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