4i3b
Crystal structure of fluorescent protein UnaG wild typeCrystal structure of fluorescent protein UnaG wild type
Structural highlights
Publication Abstract from PubMedThe fluorescent protein toolbox has revolutionized experimental biology. Despite this advance, no fluorescent proteins have been identified from vertebrates, nor has chromogenic ligand-inducible activation or clinical utility been demonstrated. Here, we report the cloning and characterization of UnaG, a fluorescent protein from Japanese eel. UnaG belongs to the fatty-acid-binding protein (FABP) family, and expression in eel is restricted to small-diameter muscle fibers. On heterologous expression in cell lines or mouse brain, UnaG produces oxygen-independent green fluorescence. Remarkably, UnaG fluorescence is triggered by an endogenous ligand, bilirubin, a membrane-permeable heme metabolite and clinical health biomarker. The holoUnaG structure at 1.2 A revealed a biplanar coordination of bilirubin by reversible pi-conjugation, and we used this high-affinity and high-specificity interaction to establish a fluorescence-based human bilirubin assay with promising clinical utility. UnaG will be the prototype for a versatile class of ligand-activated fluorescent proteins, with applications in research, medicine, and bioengineering. A bilirubin-inducible fluorescent protein from eel muscle.,Kumagai A, Ando R, Miyatake H, Greimel P, Kobayashi T, Hirabayashi Y, Shimogori T, Miyawaki A Cell. 2013 Jun 20;153(7):1602-11. doi: 10.1016/j.cell.2013.05.038. Epub 2013 Jun , 13. PMID:23768684[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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