2rkz

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{{STRUCTURE_2rkz| PDB=2rkz | SCENE= }}
 
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===Crystal structure of the second and third fibronectin f1 modules in complex with a fragment of staphylococcus aureus fnbpa-1===
 
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{{ABSTRACT_PUBMED_18713862}}
 
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==Disease==
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==Crystal structure of the second and third fibronectin f1 modules in complex with a fragment of staphylococcus aureus fnbpa-1==
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[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref>
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<StructureSection load='2rkz' size='340' side='right'caption='[[2rkz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[2rkz]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RKZ FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref><ref>PMID:11209058</ref><ref>PMID:15665290</ref><ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref><ref>PMID:11209058</ref><ref>PMID:15665290</ref><ref>PMID:19379667</ref> [[http://www.uniprot.org/uniprot/FNBA_STAA8 FNBA_STAA8]] Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.<ref>PMID:2521391</ref><ref>PMID:10788510</ref><ref>PMID:11736995</ref><ref>PMID:11553573</ref><ref>PMID:15234962</ref><ref>PMID:15216468</ref><ref>PMID:15897276</ref><ref>PMID:17516661</ref>
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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]] 2&#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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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==About this Structure==
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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=2rkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rkz OCA], [https://pdbe.org/2rkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rkz RCSB], [https://www.ebi.ac.uk/pdbsum/2rkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rkz ProSAT]</span></td></tr>
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[[2rkz]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKZ OCA].
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[https://omim.org/entry/601894 601894]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>
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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/rk/2rkz_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=2rkz ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Fibronectin|Fibronectin]]
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*[[Fibronectin 3D structures|Fibronectin 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:018713862</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: Bingham, R J.]]
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[[Category: Large Structures]]
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[[Category: 2f13f1]]
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[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
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[[Category: Acute phase]]
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[[Category: Bingham RJ]]
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[[Category: Beta zipper]]
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[[Category: Cell adhesion]]
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[[Category: Cell wall]]
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[[Category: Extracellular matrix]]
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[[Category: Fibrronectin]]
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[[Category: Glycoprotein]]
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[[Category: Heparin-binding]]
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[[Category: Peptidoglycan-anchor]]
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[[Category: Phosphorylation]]
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[[Category: Pyrrolidone carboxylic acid]]
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[[Category: Secreted]]
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[[Category: Staphylococcus aureus]]
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[[Category: Sulfation]]
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[[Category: Virulence]]
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Current revision

Crystal structure of the second and third fibronectin f1 modules in complex with a fragment of staphylococcus aureus fnbpa-1

PDB ID 2rkz

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