1qo6

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[[Image:1qo6.gif|left|200px]]
 
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==Solution structure of a pair of modules from the gelatin-binding domain of fibronectin==
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The line below this paragraph, containing "STRUCTURE_1qo6", creates the "Structure Box" on the page.
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<StructureSection load='1qo6' size='340' side='right'caption='[[1qo6]]' 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'>[[1qo6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QO6 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</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=1qo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo6 OCA], [https://pdbe.org/1qo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qo6 RCSB], [https://www.ebi.ac.uk/pdbsum/1qo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qo6 ProSAT]</span></td></tr>
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{{STRUCTURE_1qo6| PDB=1qo6 | SCENE= }}
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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/qo/1qo6_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=1qo6 ConSurf].
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<div style="clear:both"></div>
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'''SOLUTION STRUCTURE OF A PAIR OF MODULES FROM THE GELATIN-BINDING DOMAIN OF FIBRONECTIN'''
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==See Also==
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*[[Fibronectin 3D structures|Fibronectin 3D structures]]
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== References ==
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==Overview==
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<references/>
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BACKGROUND: Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen. RESULTS: The solution structure of the 101-residue 6F1 1F2 module pair, which has a weak affinity for gelatin, has been determined by multidimensional NMR spectroscopy. The tertiary structures determined for each module conform to the F1 and F2 consensus folds established previously. The experimental data suggest that the two modules interact via a small hydrophobic interface but may not be tightly associated. Near-random-coil 1H NMR chemical shifts and fast dynamics for backbone atoms in the linker indicate that this region is unlikely to be involved in the overall stabilisation of the module pair. CONCLUSIONS: The modules in the 6F1 1F2 module pair interact with each other via a flexible linker and a hydrophobic patch, which lies on the opposite side of the 1F2 module to the putative collagen-binding site. The intermodule interaction is relatively weak and transient.
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__TOC__
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</StructureSection>
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==About this Structure==
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1QO6 is a [[Single protein]] structure of 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=1QO6 OCA].
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==Reference==
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Solution structure of a pair of modules from the gelatin-binding domain of fibronectin., Bocquier AA, Potts JR, Pickford AR, Campbell ID, Structure. 1999 Dec 15;7(12):1451-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10647176 10647176]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bocquier, A A.]]
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[[Category: Bocquier AA]]
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[[Category: Campbell, I D.]]
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[[Category: Campbell ID]]
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[[Category: Pickford, A R.]]
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[[Category: Pickford AR]]
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[[Category: Potts, J R.]]
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[[Category: Potts JR]]
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[[Category: Fibronectin module pair]]
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[[Category: Gelatin-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:30:34 2008''
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Current revision

Solution structure of a pair of modules from the gelatin-binding domain of fibronectin

PDB ID 1qo6

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