2omy

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{{STRUCTURE_2omy| PDB=2omy | SCENE= }}
 
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===Crystal structure of InlA S192N/hEC1 complex===
 
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{{ABSTRACT_PUBMED_17540170}}
 
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==Disease==
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==Crystal structure of InlA S192N/hEC1 complex==
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[[http://www.uniprot.org/uniprot/CADH1_HUMAN CADH1_HUMAN]] Defects in CDH1 are the cause of hereditary diffuse gastric cancer (HDGC) [MIM:[http://omim.org/entry/137215 137215]]. An autosomal dominant cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. Note=Heterozygous germline mutations CDH1 are responsible for familial cases of diffuse gastric cancer. Somatic mutations in the has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer.<ref>PMID:10319582</ref><ref>PMID:12216071</ref> Defects in CDH1 are a cause of susceptibility to endometrial cancer (ENDMC) [MIM:[http://omim.org/entry/608089 608089]]. Defects in CDH1 are a cause of susceptibility to ovarian cancer (OC) [MIM:[http://omim.org/entry/167000 167000]]. Ovarian cancer common malignancy originating from ovarian tissue. Although many histologic types of ovarian neoplasms have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
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<StructureSection load='2omy' size='340' side='right'caption='[[2omy]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2omy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OMY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2omy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2omy OCA], [https://pdbe.org/2omy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2omy RCSB], [https://www.ebi.ac.uk/pdbsum/2omy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2omy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/INLA_LISMO INLA_LISMO] Mediates the entry of L.monocytogenes into cells.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/2omy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2omy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In causing disease, pathogens outmaneuver host defenses through a dedicated arsenal of virulence determinants that specifically bind or modify individual host molecules. This dedication limits the intruder to a defined range of hosts. Newly emerging diseases mostly involve existing pathogens whose arsenal has been altered to allow them to infect previously inaccessible hosts. We have emulated this chance occurrence by extending the host range accessible to the human pathogen Listeria monocytogenes by the intestinal route to include the mouse. Analyzing the recognition complex of the listerial invasion protein InlA and its human receptor E-cadherin, we postulated and verified amino acid substitutions in InlA to increase its affinity for E-cadherin. Two single substitutions increase binding affinity by four orders of magnitude and extend binding specificity to include formerly incompatible murine E-cadherin. By rationally adapting a single protein, we thus create a versatile murine model of human listeriosis.
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==Function==
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Extending the host range of Listeria monocytogenes by rational protein design.,Wollert T, Pasche B, Rochon M, Deppenmeier S, van den Heuvel J, Gruber AD, Heinz DW, Lengeling A, Schubert WD Cell. 2007 Jun 1;129(5):891-902. PMID:17540170<ref>PMID:17540170</ref>
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[[http://www.uniprot.org/uniprot/INLA_LISMO INLA_LISMO]] Mediates the entry of L.monocytogenes into cells. [[http://www.uniprot.org/uniprot/CADH1_HUMAN CADH1_HUMAN]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.<ref>PMID:16417575</ref> E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.<ref>PMID:16417575</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2omy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OMY OCA].
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</div>
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<div class="pdbe-citations 2omy" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Cadherin|Cadherin]]
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*[[Cadherin 3D structures|Cadherin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017540170</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Listeria monocytogenes]]
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[[Category: Large Structures]]
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[[Category: Heinz, D W.]]
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[[Category: Listeria monocytogenes EGD-e]]
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[[Category: Schubert, W D.]]
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[[Category: Heinz DW]]
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[[Category: Wollert, T.]]
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[[Category: Schubert WD]]
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[[Category: Adhesion protein]]
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[[Category: Wollert T]]
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[[Category: Cell invasion-cell adhesion complex]]
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[[Category: Ig-like domain]]
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[[Category: Invasion protein]]
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[[Category: Leucine-rich-repeat]]
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Current revision

Crystal structure of InlA S192N/hEC1 complex

PDB ID 2omy

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