3zrz

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[[Image:3zrz.png|left|200px]]
 
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==Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of Streptococcus pyogenes SfbI-5==
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The line below this paragraph, containing "STRUCTURE_3zrz", creates the "Structure Box" on the page.
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<StructureSection load='3zrz' size='340' side='right'caption='[[3zrz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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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'>[[3zrz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZRZ 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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_3zrz| PDB=3zrz | SCENE= }}
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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=3zrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zrz OCA], [https://pdbe.org/3zrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zrz RCSB], [https://www.ebi.ac.uk/pdbsum/3zrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zrz ProSAT]</span></td></tr>
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically-disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended tandem beta-zipper interaction on binding to the N-terminal domain of Fn. Several FnBR residues are highly conserved across bacterial species, and here we investigate their contribution to the interaction. Mutation of these residues to alanine in SfbI-5 (a disordered FnBR from the human pathogen Streptococcus pyogenes) reduced binding but for each residue the change in free energy of binding was &lt;2 kcal/mol. The structure of an SfbI-5 peptide in complex with the second and third F1 modules from Fn confirms that the conserved FnBR residues play equivalent functional roles across bacterial species. Thus, in SfbI-5, the binding energy for the tandem beta-zipper interaction with Fn is distributed across the interface rather than concentrated in a small number of ''hot spot'' residues that are frequently observed in the interactions of folded proteins. We propose that this might be a common feature of the interactions of IDRs, and is likely to pose a challenge for the development of small molecule inhibitors of FnBP-mediated adhesion to and invasion of host cells.
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===CRYSTAL STRUCTURE OF THE SECOND AND THIRD FIBRONECTIN F1 MODULES IN COMPLEX WITH A FRAGMENT OF STREPTOCOCCUS PYOGENES SFBI-5===
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Structural and functional analysis of the tandem {beta}-zipper interaction of a streptococcal protein with human fibronectin.,Norris NC, Bingham RJ, Harris G, Speakman A, Jones RP, Leech A, Turkenburg JP, Potts JR J Biol Chem. 2011 Aug 12. PMID:21840989<ref>PMID:21840989</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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<div class="pdbe-citations 3zrz" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21840989}}, adds the Publication Abstract to the page
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*[[Fibronectin 3D structures|Fibronectin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21840989 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21840989}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3zrz]] is a 4 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=3ZRZ OCA].
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==Reference==
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<ref group="xtra">PMID:021840989</ref><references group="xtra"/>
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[[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: Norris, N C.]]
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[[Category: Streptococcus pyogenes]]
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[[Category: Potts, J R.]]
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[[Category: Bingham RJ]]
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[[Category: Beta zipper]]
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[[Category: Norris NC]]
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[[Category: Cell adhesion]]
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[[Category: Potts JR]]
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[[Category: Prtf]]
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Current revision

Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of Streptococcus pyogenes SfbI-5

PDB ID 3zrz

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