View source for 6gbg


==Helicobacter pylori adhesin HopQ type I bound to the N-terminal domain of human CEACAM1==
<StructureSection load='6gbg' size='340' side='right'caption='[[6gbg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gbg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_G27 Helicobacter pylori G27] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GBG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></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=6gbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbg OCA], [https://pdbe.org/6gbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gbg RCSB], [https://www.ebi.ac.uk/pdbsum/6gbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEAM1_HUMAN CEAM1_HUMAN] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6gbg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori G27]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gerhard M]]
[[Category: Kruse T]]
[[Category: Moonens K]]
[[Category: Remaut H]]