Sandbox Q123: Difference between revisions
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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]]) '> | <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]]) '> | ||
== Structural insights == | |||
<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). | |||
This is a test, <scene name='93/932569/297-307_space_fill/1'>Space Fill 297-307</scene>, of FN. | |||
== 3D Structures of Fibronectin == | |||
[[Fibronectin 3D structures]] | |||
</StructureSection> | |||
== Function == | == Function == | ||
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Overexpression of Fn1 is associated with lung cancer<ref>PMID:16397245</ref>. | Overexpression of Fn1 is associated with lung cancer<ref>PMID:16397245</ref>. | ||
== References == | == References == | ||
Revision as of 06:48, 10 November 2022
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Function
Fibronectin 3D structures (Fn) is a glycoprotein which binds extracellular matrix components like integrin, collagen, fibrin and others. It plays an important role in cell adhesion, migration and differentiation[1][2]. In addition, Fn is also important for the adherence of pathogens to host tissues and the linking between proteins and cells[3].
Relevance
Fn is associated with wound healing. Fn is a potential marker for radiation resistance.
Disease
Overexpression of Fn1 is associated with lung cancer[4].
References
- ↑ Pankov R, Yamada KM. Fibronectin at a glance. J Cell Sci. 2002 Oct 15;115(Pt 20):3861-3. PMID:12244123
- ↑ Proctor RA. Fibronectin: a brief overview of its structure, function, and physiology. Rev Infect Dis. 1987 Jul-Aug;9 Suppl 4:S317-21. doi:, 10.1093/clinids/9.supplement_4.s317. PMID:3326130 doi:https://dx.doi.org/10.1093/clinids/9.supplement_4.s317
- ↑ Mosher DF. Physiology of fibronectin. Annu Rev Med. 1984;35:561-75. doi: 10.1146/annurev.me.35.020184.003021. PMID:6326663 doi:https://dx.doi.org/10.1146/annurev.me.35.020184.003021
- ↑ 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:https://dx.doi.org/10.1158/0008-5472.CAN-05-2367
