6d38

Photodissociable dimeric Dronpa green fluorescent protein variant M (pdDronpaM)

spinqualitylabelsall models 6d38, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6d38 is a 1 chain structure with sequence from Echinophyllia sp. SC22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: GYC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5TLG6_9CNID Publication Abstract from PubMed Protein kinases transduce signals to regulate a wide array of cellular functions in eukaryotes. A generalizable method for optical control of kinases would enable fine spatiotemporal interrogation or manipulation of these various functions. We report the design and application of single-chain cofactor-free kinases with photoswitchable activity. We engineered a dimeric protein, pdDronpa, that dissociates in cyan light and reassociates in violet light. Attaching two pdDronpa domains at rationally selected locations in the kinase domain, we created the photoswitchable kinases psRaf1, psMEK1, psMEK2, and psCDK5. Using these photoswitchable kinases, we established an all-optical cell-based assay for screening inhibitors, uncovered a direct and rapid inhibitory feedback loop from ERK to MEK1, and mediated developmental changes and synaptic vesicle transport in vivo using light. Optical control of cell signaling by single-chain photoswitchable kinases.,Zhou XX, Fan LZ, Li P, Shen K, Lin MZ Science. 2017 Feb 24;355(6327):836-842. doi: 10.1126/science.aah3605. PMID:28232577 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dronpa Green Fluorescent Protein 3D structures

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