3m7p

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{{Seed}}
 
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[[Image:3m7p.jpg|left|200px]]
 
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==Fibronectin fragment==
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The line below this paragraph, containing "STRUCTURE_3m7p", creates the "Structure Box" on the page.
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<StructureSection load='3m7p' size='340' side='right'caption='[[3m7p]], [[Resolution|resolution]] 2.50&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'>[[3m7p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M7P 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]] 2.5&#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=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3m7p| PDB=3m7p | 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=3m7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7p OCA], [https://pdbe.org/3m7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m7p RCSB], [https://www.ebi.ac.uk/pdbsum/3m7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7p 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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== 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/m7/3m7p_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=3m7p 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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Fibronectin is a modular extracellular matrix protein involved in cell adhesion, cell motility, wound healing, and maintenance of cell morphology. It is composed of multiple repeats of three distinct modules: F(I), F(II), and F(III). Various combinations of these modules create fragments able to interact with different constituents of the extracellular matrix. Here, we present the 2.5-A resolution crystal structure of its 45-kDa gelatin-binding domain (GBD; 6F(I)-1F(II)-2F(II)-7F(I)-8F(I)-9F(I)), which also corresponds to the C-terminal half of the migration stimulating factor, a Fn splice variant expressed in human breast cancers. GBD forms a very compact zinc-mediated homodimer, in stark contrast with previous structures of fibronectin fragments. Most remarkably, 8F(I) no longer adopts the canonical F(I) fold but is composed of two long strands that associate with 7F(I) and 9F(I) into a large beta-sheet superdomain. Binding studies in solution confirmed that Zn induces conformational rearrangements and causes loss of binding of Fn-GBD to high-affinity collagen peptides. These data suggest the Zn may play a regulatory role for the cellular functions of fibronectin.
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===Fibronectin fragment===
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Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding.,Graille M, Pagano M, Rose T, Ravaux MR, van Tilbeurgh H Structure. 2010 Jun 9;18(6):710-8. PMID:20541508<ref>PMID:20541508</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 3m7p" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20541508}}, adds the Publication Abstract to the page
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*[[Fibronectin|Fibronectin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20541508 is the PubMed ID number.
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*[[Fibronectin 3D structures|Fibronectin 3D structures]]
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*[[Sandbox Q123|Sandbox Q123]]
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{{ABSTRACT_PUBMED_20541508}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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3M7P is a 1 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=3M7P OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:20541508</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Graille, M.]]
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[[Category: Large Structures]]
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[[Category: Pagano, M.]]
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[[Category: Graille M]]
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[[Category: Ravaux, M Reboud.]]
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[[Category: Pagano M]]
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[[Category: Rose, T.]]
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[[Category: Reboud Ravaux M]]
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[[Category: Tilbeurgh, H van.]]
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[[Category: Rose T]]
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[[Category: Cell adhesion]]
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[[Category: Van Tilbeurgh H]]
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[[Category: Conformational change]]
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[[Category: Dimer]]
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[[Category: Extracellular matrix]]
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[[Category: Fibronectin]]
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[[Category: Modular protein]]
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[[Category: Zinc binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 23 08:50:43 2010''
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Current revision

Fibronectin fragment

PDB ID 3m7p

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