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Fibronectin

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<StructureSection load='3m7p' size='350' side='right' scene='' caption='Human glycosylated fibronectin gelatin-binding domain complex with PEG400, dodecaethylene glycol and Zn+2 ions (grey) (PDB code [[3m7p]]) '>
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<StructureSection load='3m7p' size='350' side='right' scene='43/430871/Cv/2' caption='Human glycosylated fibronectin gelatin-binding domain complex with PEG400, dodecaethylene glycol and Zn+2 ions (grey) (PDB code [[3m7p]]) '>
== Function ==
== Function ==
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== Disease ==
== Disease ==
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Overexpression of Fn1 is associated with lung cancer.
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Overexpression of Fn1 is associated with lung cancer<ref>PMID:16397245</ref>.
== Structural insights ==
== Structural insights ==
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Fn is a dimer of homologous monomers linked by S-S bond. Each monomer contains 3 types of modules: FnI, FnII and FnIII. Each module contains several numbered protein binding domains, i.e., FnI<sub>6</sub>-FnII<sub>1-2</sub>-FnI<sub>7-9</sub> is the gelatin binding domain (GBD).
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<scene name='43/430871/Cv/3'>Fn is a dimer of homologous monomers</scene> linked by S-S bond. Each monomer contains 3 types of modules: FnI, FnII and FnIII. Each module contains several numbered protein binding domains, i.e., FnI<sub>6</sub>-FnII<sub>1-2</sub>-FnI<sub>7-9</sub> is the gelatin binding domain (GBD).
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</StructureSection>
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== 3D Structures of Fibronectin ==
== 3D Structures of Fibronectin ==
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[[Fibronectin 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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* Fn module FnI
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**[[3m7p]] – hFn GBD – human<br />
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**[[1e8b]], [[1e88]], [[1qo6]] - hFn GBD – NMR<br />
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**[[3gxe]], [[3ejh]] – hFnI<sub>8-9</sub> +collagen alpha-1<br />
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**[[1fbr]] - hFnI<sub>4-5</sub> - NMR<br />
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**[[2rky]], [[2rl0]] – hFnI<sub>4-5</sub>+Fn binding peptide<br />
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**[[2rkz]], [[3cal]], [[3zrz]] - hFn<sub>2-3</sub> +Fn binding peptide<br />
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**[[2cg6]], [[2cg7]] - hFnI<sub>2-3</sub><br />
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**[[2cku]] - hFnI<sub>2-3</sub> – NMR<br />
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**[[1o9a]] - hFnI<sub>1-2</sub>+B3 from FNBB – NMR<br />
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**[[2ec3]] – hFnI<sub>11</sub> – NMR<br />
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**[[3r8q]] – hFnI<sub>12-14</sub><br />
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**[[1qgb]] – hFn FnI N-terminal - NMR<br />
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**[[2ck2]] – hFn (mutant) core swapped<br />
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**[[1j8k]] – hFn extra domain 2 – NMR<br />
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**[[1fnh]] – hFn heparin and integrin binding domains<br />
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**[[2qbw]], [[3ch8]] – hFn-PDZ fusion<br />
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**[[4gh7]] – hFn residues 1173-1448 + Neutrophil gelatinase-associated lipocalin
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* Fn module FnII
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**[[2fn2]] – hFnII<sub>2</sub> – NMR
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* Fn module FnIII
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**[[1q38]], [[1x3d]], [[1x4x]], [[1x5x]] - hFn FnIII – NMR<br />
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**[[2h41]], [[2h45]] – hFnIII<sub>2</sub> – NMR<br />
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**[[1oww]] - hFnIII<sub>1</sub> – NMR<br />
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**[[2ha1]] - hFnIII<sub>1-2</sub> – NMR<br />
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**[[2crm]] - hFnIII<sub>4</sub> – NMR<br />
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**[[2crz]] - hFnIII<sub>5</sub> – NMR<br />
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**[[1fna]], [[1ttf]], [[1ttg]] – hFnIII<sub>10</sub><br />
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**[[4mmx]] - hFnIII<sub>10</sub> + integrin α V + integrin β 3<br />
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**[[4mmy]], [[4mmz]] - hFnIII<sub>10</sub> (mutant) + integrin α V + integrin β 3<br />
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**[[2ocf]] - hFnIII<sub>10</sub>+estrogen receptor ligand-binding domain<br />
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**[[1fnf]] – hFnIII<sub>7-10</sub><br />
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**[[2fnb]] – hFn FnIII ed-b domain – NMR<br />
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**[[1mfn]], [[2mfn]] – FnIII<sub>9-10</sub> – mouse - NMR<br />
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**[[2vmg]], [[2vmi]] - Fn FnIII carbohydrate-binding domain – ''Clostridium perfringens''
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* Fn module FnI+FnII
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**[[3mql]] – hFnI<sub>6</sub>+FnII<sub>2</sub>+FnI<sub>7</sub>
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human glycosylated fibronectin gelatin-binding domain complex with PEG400, dodecaethylene glycol and Zn+2 ions (grey) (PDB code 3m7p)

Drag the structure with the mouse to rotate

References

  1. ↑ Pankov R, Yamada KM. Fibronectin at a glance. J Cell Sci. 2002 Oct 15;115(Pt 20):3861-3. PMID:12244123
  2. ↑ Han S, Khuri FR, Roman J. Fibronectin stimulates non-small cell lung carcinoma cell growth through activation of Akt/mammalian target of rapamycin/S6 kinase and inactivation of LKB1/AMP-activated protein kinase signal pathways. Cancer Res. 2006 Jan 1;66(1):315-23. PMID:16397245 doi:http://dx.doi.org/10.1158/0008-5472.CAN-05-2367

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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