2fvn

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{{Seed}}
 
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[[Image:2fvn.png|left|200px]]
 
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==The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins==
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The line below this paragraph, containing "STRUCTURE_2fvn", creates the "Structure Box" on the page.
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<StructureSection load='2fvn' size='340' side='right'caption='[[2fvn]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2fvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FVN FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=2fvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvn OCA], [https://pdbe.org/2fvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fvn RCSB], [https://www.ebi.ac.uk/pdbsum/2fvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fvn ProSAT]</span></td></tr>
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{{STRUCTURE_2fvn| PDB=2fvn | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AFAD_ECOLX AFAD_ECOLX]
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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/fv/2fvn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fvn 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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Afa/Dr family of adhesins are produced by pathogenic Escherichia coli strains that are especially prevalent in chronic diarrhoeal and recurrent urinary tract infections. Most notably, they are found in up to 50% of cystitis cases in children and 30% of pyelonephritis in pregnant women. Afa/Dr adhesins are capped surface fibrils that mediate recognition of the host and subsequent bacterial internalization. Using the newly solved three-dimensional structure of the minimal invasive complex (AfaDE) combined with biochemical and cellular assays, we reveal the architecture of the fibrillar cap and identify a novel mode of synergistic integrin recognition.
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===The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins===
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The solution structure of the invasive tip complex from Afa/Dr fibrils.,Cota E, Jones C, Simpson P, Altroff H, Anderson KL, du Merle L, Guignot J, Servin A, Le Bouguenec C, Mardon H, Matthews S Mol Microbiol. 2006 Oct;62(2):356-66. Epub 2006 Sep 8. PMID:16965519<ref>PMID:16965519</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16965519}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2fvn" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16965519 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16965519}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2FVN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVN OCA].
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==Reference==
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The solution structure of the invasive tip complex from Afa/Dr fibrils., Cota E, Jones C, Simpson P, Altroff H, Anderson KL, du Merle L, Guignot J, Servin A, Le Bouguenec C, Mardon H, Matthews S, Mol Microbiol. 2006 Oct;62(2):356-66. Epub 2006 Sep 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16965519 16965519]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Anderson, K L.]]
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[[Category: Anderson KL]]
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[[Category: Cota, E.]]
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[[Category: Cota E]]
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[[Category: Matthews, S J.]]
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[[Category: Matthews SJ]]
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[[Category: Simpson, P.]]
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[[Category: Simpson P]]
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[[Category: Afad]]
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[[Category: Afae]]
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[[Category: Afimbrial]]
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[[Category: Ceacam]]
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[[Category: Daec]]
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[[Category: Daf]]
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[[Category: Fibrillar]]
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[[Category: Integrin-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:21:06 2008''
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Current revision

The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins

PDB ID 2fvn

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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