Please use this identifier to cite or link to this item: http://hdl.handle.net/10125/47312

Recombinant expression in E. coli of human FGFR2 with its transmembrane and extracellular domains

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Title:Recombinant expression in E. coli of human FGFR2 with its transmembrane and extracellular domains
Authors:Bajinting, Adam
Ng, Ho Leung
Keywords:Biochemistry
Cancer--Research
Date Issued:2017
Publisher:PeerJ
Citation:Bajinting and Ng (2017), Recombinant expression in E. coli of human FGFR2 with its transmembrane and extracellular domains. PeerJ 5:e3512; DOI 10.7717/peerj.3512
Relation:https://peerj.com/articles/3512/
Abstract:Fibroblast growth factor receptors (FGFRs) are a family of receptor tyrosine kinases containing three domains: an extracellular receptor domain, a single transmembrane helix, and an intracellular tyrosine kinase domain. FGFRs are activated by fibroblast growth factors (FGFs) as part of complex signal transduction cascades regulating angiogenesis, skeletal formation, cell differentiation, proliferation, cell survival, and cancer. We have developed the first recombinant expression system in E. coli to produce a construct of human FGFR2 containing its transmembrane and extracellular receptor domains. We demonstrate that the expressed construct is functional in binding heparin and dimerizing. Size exclusion chromatography demonstrates that the purified FGFR2 does not form a complex with FGF1 or adopts an inactive dimer conformation. Progress towards the successful recombinant production of intact FGFRs will facilitate further biochemical experiments and structure determination that will provide insight into how extracellular FGF binding activates intracellular kinase activity.
Description:Research article
Pages/Duration:14
URI/DOI:http://hdl.handle.net/10125/47312
DOI:10.7717/peerj.3512
Rights:Creative Commons CC-BY 4.0
Appears in Collections: Ng, Ho Leung


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