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==Crystal structure of the TNF-alpha inducing protein (Tip alpha) from Helicobacter pylori== | |||
<StructureSection load='3gio' size='340' side='right'caption='[[3gio]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3gio]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GIO 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3gio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gio OCA], [https://pdbe.org/3gio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gio RCSB], [https://www.ebi.ac.uk/pdbsum/3gio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gio ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Helicobacter pylori infection is one of the highest risk factors for gastroduodenal diseases including gastric cancer. Tumor necrosis factor-alpha (TNF-alpha) is one of the essential cytokines for tumor promotion, and thus, an H. pylori protein that induces TNF-alpha is believed to play a significant role in gastric cancer development in humans. The HP0596 gene product of H. pylori strain 26695 was identified as the TNF-alpha-inducing protein (Tipalpha). Tipalpha is secreted from H. pylori as dimers and enters the gastric cells. It was shown to have a DNA-binding activity. Here, we have determined the crystal structure of Tipalpha from H. pylori. Its monomer consists of two structural domains ("mixed domain" and "helical domain"). Tipalpha exists as a dimer in the crystal, and the dimeric structure represents a novel scaffold for DNA binding. A positively charged surface patch formed across the two monomers of the Tipalpha dimer by the loop between helices alpha1 and alpha2 may be important in DNA binding. | |||
Crystal structure of the TNF-alpha-Inducing protein (Tipalpha) from Helicobacter pylori: Insights into Its DNA-binding activity.,Jang JY, Yoon HJ, Yoon JY, Kim HS, Lee SJ, Kim KH, Kim do J, Jang S, Han BG, Lee BI, Suh SW J Mol Biol. 2009 Sep 11;392(1):191-7. Epub 2009 Jul 10. PMID:19596016<ref>PMID:19596016</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3gio" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Han | [[Category: Large Structures]] | ||
[[Category: Jang | [[Category: Han BG]] | ||
[[Category: Jang | [[Category: Jang JY]] | ||
[[Category: Kim | [[Category: Jang S]] | ||
[[Category: Kim | [[Category: Kim DJ]] | ||
[[Category: Kim | [[Category: Kim HS]] | ||
[[Category: Lee | [[Category: Kim KH]] | ||
[[Category: Lee | [[Category: Lee BI]] | ||
[[Category: Suh | [[Category: Lee SJ]] | ||
[[Category: Yoon | [[Category: Suh SW]] | ||
[[Category: Yoon | [[Category: Yoon HJ]] | ||
[[Category: Yoon JY]] | |||