Fibronectin: Difference between revisions

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</StructureSection>
</StructureSection>


== 3D Structures of Fibronectin ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
* Fn module FnI
**[[3m7p]] – hFn GBD – human<br />
**[[1e8b]], [[1e88]], [[1qo6]] - hFn GBD – NMR<br />
**[[3gxe]], [[3ejh]] – hFnI<sub>8-9</sub> +collagen alpha-1<br />
**[[1fbr]] - hFnI<sub>4-5</sub> - NMR<br />
**[[2rky]], [[2rl0]] – hFnI<sub>4-5</sub>+Fn binding peptide<br />
**[[2rkz]], [[3cal]], [[3zrz]] - hFn<sub>2-3</sub> +Fn binding peptide<br />
**[[2cg6]], [[2cg7]] - hFnI<sub>2-3</sub><br />
**[[2cku]] - hFnI<sub>2-3</sub> – NMR<br />
**[[1o9a]] - hFnI<sub>1-2</sub>+B3 from FNBB – NMR<br />
**[[2ec3]] – hFnI<sub>11</sub> – NMR<br />
**[[3r8q]] – hFnI<sub>12-14</sub><br />
**[[1qgb]] – hFn FnI N-terminal - NMR<br />
**[[2ck2]] – hFn (mutant) core swapped<br />
**[[1j8k]] – hFn extra domain 2 – NMR<br />
**[[1fnh]] – hFn heparin and integrin binding domains<br />
**[[2qbw]], [[3ch8]] – hFn-PDZ fusion<br />
**[[4gh7]] – hFn residues 1173-1448 + Neutrophil gelatinase-associated lipocalin
* Fn module FnII
**[[2fn2]] – hFnII<sub>2</sub> – NMR
* Fn module FnIII
**[[1q38]], [[1x3d]], [[1x4x]], [[1x5x]] - hFn FnIII – NMR<br />
**[[2h41]], [[2h45]] – hFnIII<sub>2</sub> – NMR<br />
**[[1oww]] - hFnIII<sub>1</sub> – NMR<br />
**[[2ha1]] - hFnIII<sub>1-2</sub> – NMR<br />
**[[2crm]] - hFnIII<sub>4</sub> – NMR<br />
**[[2crz]] - hFnIII<sub>5</sub> – NMR<br />
**[[4lxo]] - hFn 9-10FnIII <br />
**[[1fna]], [[1ttf]], [[1ttg]] – hFnIII<sub>10</sub><br />
**[[4mmx]] - hFnIII<sub>10</sub> + integrin α V + integrin β 3<br />
**[[4mmy]], [[4mmz]] - hFnIII<sub>10</sub> (mutant) + integrin α V + integrin β 3<br />
**[[2ocf]] - hFnIII<sub>10</sub>+estrogen receptor ligand-binding domain<br />
**[[1fnf]] – hFnIII<sub>7-10</sub><br />
**[[5dft]] - hFn FnIII<sub>11</sub> <br />
**[[6hnf]] - hFn 14FnIII - NMR <br />
**[[5m0a]] - hFn 15FnIII - NMR <br />
**[[2fnb]] – hFn FnIII ed-b domain – NMR<br />
**[[1mfn]], [[2mfn]] – FnIII<sub>9-10</sub> – mouse - NMR<br />
**[[2vmg]], [[2vmi]] - Fn FnIII carbohydrate-binding domain – ''Clostridium perfringens''
* Fn module FnI+FnII
**[[3mql]] – hFnI<sub>6</sub>+FnII<sub>2</sub>+FnI<sub>7</sub>
*Fn
**[[5n48]], [[5n47]] – hFn residues 1266-1357 + NGAL<br />
**[[5dc0]] - hFn residues 1-93 + Abl1 <br />
}}
== References ==
== References ==
<references/>
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:14, 1 July 2019


Function

Fibronectin (Fn) is a glycoprotein which binds extracellular matrix components like integrin, collagen, fibrin and others. It is a component of cell adhesion[1].

Relevance

Fn is associated with wound healing. Fn is a potential marker for radiation resistance.

Disease

Overexpression of Fn1 is associated with lung cancer[2].

Structural insights

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., FnI6-FnII1-2-FnI7-9 is the gelatin binding domain (GBD).

3D Structures of Fibronectin

Fibronectin 3D structures


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

ReferencesReferences

  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

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Alexander Berchansky, Michal Harel
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