Fibronectin

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[[Image:1fbr.png|left|200px|thumb|Crystal Structure of Fibronectin 4-5FnI fragment [[1fbr]]]]
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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]]) '>
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{{STRUCTURE_3m7p| PDB=3m7p | SIZE=400| SCENE= |right|CAPTION=Human fibronectin gelatin-binding domain complex with PEG400, dodecaethylene glycol and Zn+2 ions [[3m7p]] }}
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== Function ==
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[[Fibronectin]] (Fn) is a glycoprotein which binds extracellular matrix components like integrin, collagen, fibrin and others. It is a component of cell adhesion<ref>PMID:12244123</ref>.
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== Relevance ==
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Fn is associated with wound healing. Fn is a potential marker for radiation resistance.
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== Disease ==
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Overexpression of Fn1 is associated with lung cancer<ref>PMID:16397245</ref>.
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== Structural insights ==
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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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[[Fibronectin]] (Fn) is a glycoprotein which binds extracellular matrix components like integrin, collagen, fibrin and others. It is a component of cell adhesion. It 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., 6FnI+1-2FnII is the gelatin binding domain (GBD). The images at the left and at the right correspond to one representative Fn, ''i.e.'' the crystal structure of human Fibronectin 4-5FnI fragment ([[1fbr]]).
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{{TOC limit|limit=2}}
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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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=== 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]] – hFn 8-9FnI+collagen alpha-1<br />
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[[1fbr]] - hFn 4-5FnI - NMR<br />
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[[2rky]], [[2rl0]] – hFn 4-5FnI+Fn binding peptide<br />
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[[2rkz]], [[3cal]], [[3zrz]] - hFn 2-3FnI+Fn binding peptide<br />
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[[2cg6]], [[2cg7]] - hFn 2-3FnI<br />
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[[2cku]] - hFn 2-3FnI – NMR<br />
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[[1o9a]] - hFn 1-2FnI+B3 from FNBB – NMR<br />
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[[2ec3]] – hFn 11FnI – NMR<br />
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[[3r8q]] – hFn 12-14FnI<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]] – hFn 2FnII – 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]] – hFn 2FnIII – NMR<br />
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[[1oww]] - hFn 1FnIII – NMR<br />
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[[2ha1]] - hFn 1-2FnIII – NMR<br />
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[[2crm]] - hFn 4FnIII – NMR<br />
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[[2crz]] - hFn 5FnIII – NMR<br />
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[[1fna]], [[1ttf]], [[1ttg]] – hFn 10FnIII<br />
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[[2ocf]] - hFn 10FnIII+estrogen receptor ligand-binding domain<br />
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[[1fnf]] – hFn 7-10FnIII<br />
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[[2fnb]] – hFn FnIII ed-b domain – NMR<br />
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[[1mfn]], [[2mfn]] – Fn 9-10FnIII – 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]] – hFn 6FnI+2FnII+7FnI
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== References ==
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<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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