Sandbox Q123
From Proteopedia
(Difference between revisions)
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== Structural insights == | == Structural insights == | ||
| - | <scene name='43/430871/Cv/3'>Fn is a dimer of homologous monomers</scene> linked by S-S bond. | + | <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 repeating units: FnI, FnII and FnIII. Type I and type II repeats are disulfide-bonded loops, containing about 45 and 60 amino-acids each, while type III repeats are about 90 amino-acids long without S-S bonds<ref name="Pancov">PMID:12244123</ref><ref name="Proctor">PMID:3326130</ref><ref name="Richard">PMID:3916323</ref>. 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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== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
| - | Fn is associated with wound healing. Fn is a potential marker for radiation resistance. | + | Fn is associated with inflammation area and the process of wound healing. Fn is a potential marker for radiation resistance. |
== Disease == | == Disease == | ||
Revision as of 07:19, 10 November 2022
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References
- ↑ 1.0 1.1 Pankov R, Yamada KM. Fibronectin at a glance. J Cell Sci. 2002 Oct 15;115(Pt 20):3861-3. PMID:12244123
- ↑ 2.0 2.1 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:http://dx.doi.org/10.1093/clinids/9.supplement_4.s317
- ↑ Hynes R. Molecular biology of fibronectin. Annu Rev Cell Biol. 1985;1:67-90. doi: 10.1146/annurev.cb.01.110185.000435. PMID:3916323 doi:http://dx.doi.org/10.1146/annurev.cb.01.110185.000435
- ↑ Mosher DF. Physiology of fibronectin. Annu Rev Med. 1984;35:561-75. doi: 10.1146/annurev.me.35.020184.003021. PMID:6326663 doi:http://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:http://dx.doi.org/10.1158/0008-5472.CAN-05-2367
