Conformational antibody binding to a native, cell-free expressed GPCR in block copolymer membranes.
basic_science · Level V
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- Record sourced from PubMed, PMID 25329156.
- Also identified by DOI 10.1371/journal.pone.0110847 and PMC identifier PMC2601552.
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Abstract
G-protein coupled receptors (GPCRs) play a key role in physiological processes and are attractive drug targets. Their biophysical characterization is, however, highly challenging because of their innate instability outside a stabilizing membrane and the difficulty of finding a suitable expression system. We here show the cell-free expression of a GPCR, CXCR4, and its direct embedding in diblock copolymer membranes. The polymer-stabilized CXCR4 is readily immobilized onto biosensor chips for label-free binding analysis. Kinetic characterization using a conformationally sensitive antibody shows the receptor to exist in the correctly folded conformation, showing binding behaviour that is commensurate with heterologously expressed CXCR4.